3t0f - Revision history

OCA at 13:13, 14 March 2024

OCA — Thu, 14 Mar 2024 13:13:42 GMT

←Older revision		Revision as of 13:13, 14 March 2024
Line 3:		Line 3:
	<StructureSection load='3t0f' size='340' side='right'caption='[[3t0f]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='3t0f' size='340' side='right'caption='[[3t0f]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3t0f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Ecoli Ecoli~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T0F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T0F FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3t0f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T0F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T0F FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=F3S:FE3~~-~~S4+CLUSTER'>F3S</scene>~~, ~~<scene name='pdbligand=H6P:(2E)-4-HYDROXY-3-METHYLBUT-2-EN-1-YL+TRIHYDROGEN+DIPHOSPHATE'>H6P</scene></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.9Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>~~[[~~Related_structure~~\|~~Related:~~]]~~</b></td><td class="sblockDat"><div style='overflow: auto~~; ~~max-height: 3em;'>[[3f7t\|3f7t]], [[3dnf\|3dnf]], [[3szl\|3szl]], [[3szo\|3szo]], [[3szu\|3szu]], [[3t0g\|3t0g]]</div>~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=H6P:(2E)-4-HYDROXY-3-METHYLBUT-2-EN-1-YL+TRIHYDROGEN+DIPHOSPHATE'>H6P</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>ispH, lytB, yaaE, b0029, JW0027 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~83333 ECOLI])</td~~><~~/tr>~~	+
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks'>[https~~:~~//en.wikipedia.org/wiki/4-hydroxy-3-methylbut-2~~-~~enyl_diphosphate_reductase~~ 4-~~hydroxy~~-3-~~methylbut~~-2-~~enyl diphosphate reductase], with EC number [https://www.brenda~~-~~enzymes.info/php/result_flat.php4?ecno=~~1~~.17.1.2 1.17.1.2]~~ </~~span~~></td></tr>	+
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3t0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t0f OCA], [https://pdbe.org/3t0f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t0f RCSB], [https://www.ebi.ac.uk/pdbsum/3t0f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t0f ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3t0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t0f OCA], [https://pdbe.org/3t0f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t0f RCSB], [https://www.ebi.ac.uk/pdbsum/3t0f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t0f ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/ISPH_ECOLI ISPH_ECOLI]] Converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Is also involved in penicillin tolerance and control of the stringent response. Seems to directly or indirectly interact with RelA to maintain it in an inactive form during normal growth.<ref>PMID:19569147</ref> <ref>PMID:20080550</ref> <ref>PMID:22137895</ref>	+	[https://www.uniprot.org/uniprot/ISPH_ECOLI ISPH_ECOLI] Converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Is also involved in penicillin tolerance and control of the stringent response. Seems to directly or indirectly interact with RelA to maintain it in an inactive form during normal growth.<ref>PMID:19569147</ref> <ref>PMID:20080550</ref> <ref>PMID:22137895</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Isoprenoids derive from two universal precursors, isopentenyl diphosphate and dimethylallyl diphosphate, which in most human pathogens are synthesized in the deoxyxylulose phosphate pathway. The last step of this pathway is the conversion of (E)-1-hydroxy-2-methylbut-2-enyl-4-diphosphate into a mixture of isopentenyl diphosphate and dimethylallyl diphosphate catalyzed by the iron-sulfur protein IspH. The crystal structures reported here of the IspH mutant proteins T167C, E126D and E126Q reveal an alternative substrate conformation compared to the wild-type structure. Thus, the previously observed alkoxide complex decomposes, and the substrate's hydroxymethyl group rotates to interact with Glu126. The carboxyl group of Glu126 then donates a proton to the hydroxyl group to enable water elimination. The structural and functional studies provide further knowledge of the IspH reaction mechanism, which opens up new routes to inhibitor design against malaria and tuberculosis.	+
-		+
-	Crystal Structures of Mutant IspH Proteins Reveal a Rotation of the Substrate's Hydroxymethyl Group during Catalysis.,Span I, Grawert T, Bacher A, Eisenreich W, Groll M J Mol Biol. 2011 Nov 23. PMID:22137895<ref>PMID:22137895</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 3t0f" style="background-color:#fffaf0;"></div~~>	+

	==See Also==		==See Also==
Line 28:		Line 17:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: 4-~~hydroxy-3-methylbut-2-enyl diphosphate reductase]]~~	+	[[Category: Escherichia coli K-12]]
-	~~[[Category: Ecoli~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bacher, A]]	+	[[Category: Bacher A]]
-	[[Category: Eisenreich, W]]	+	[[Category: Eisenreich W]]
-	[[Category: Graewert, T]]	+	[[Category: Graewert T]]
-	[[Category: Groll, M]]	+	[[Category: Groll M]]
-	[[Category: Span, I]]	+	[[Category: Span I]]
-	~~[[Category: 3fe-4s iron-sulfur cluster]]~~	+
-	~~[[Category: Conserved cysteine]]~~	+
-	~~[[Category: Ipp and dmapp production final step]]~~	+
-	~~[[Category: Low activity]]~~	+
-	~~[[Category: Non-mevalonate pathway]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Substrate hmbpp~~]]	+

OCA at 16:37, 6 July 2022

OCA — Wed, 06 Jul 2022 16:37:56 GMT

←Older revision		Revision as of 16:37, 6 July 2022
Line 1:		Line 1:

	==IspH:HMBPP (substrate) structure of the E126D mutant==		==IspH:HMBPP (substrate) structure of the E126D mutant==
-	<StructureSection load='3t0f' size='340' side='right' caption='[[3t0f]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='3t0f' size='340' side='right'caption='[[3t0f]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3t0f]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T0F OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3T0F FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3t0f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T0F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T0F FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=H6P:(2E)-4-HYDROXY-3-METHYLBUT-2-EN-1-YL+TRIHYDROGEN+DIPHOSPHATE'>H6P</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=H6P:(2E)-4-HYDROXY-3-METHYLBUT-2-EN-1-YL+TRIHYDROGEN+DIPHOSPHATE'>H6P</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3f7t\|3f7t]], [[3dnf\|3dnf]], [[3szl\|3szl]], [[3szo\|3szo]], [[3szu\|3szu]], [[3t0g\|3t0g]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3f7t\|3f7t]], [[3dnf\|3dnf]], [[3szl\|3szl]], [[3szo\|3szo]], [[3szu\|3szu]], [[3t0g\|3t0g]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ispH, lytB, yaaE, b0029, JW0027 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ispH, lytB, yaaE, b0029, JW0027 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/4-hydroxy-3-methylbut-2-enyl_diphosphate_reductase 4-hydroxy-3-methylbut-2-enyl diphosphate reductase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.1.2 1.17.1.2] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/4-hydroxy-3-methylbut-2-enyl_diphosphate_reductase 4-hydroxy-3-methylbut-2-enyl diphosphate reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.1.2 1.17.1.2] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3t0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t0f OCA], [~~http~~://pdbe.org/3t0f PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3t0f RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3t0f PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3t0f ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3t0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t0f OCA], [https://pdbe.org/3t0f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t0f RCSB], [https://www.ebi.ac.uk/pdbsum/3t0f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t0f ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/ISPH_ECOLI ISPH_ECOLI]] Converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Is also involved in penicillin tolerance and control of the stringent response. Seems to directly or indirectly interact with RelA to maintain it in an inactive form during normal growth.<ref>PMID:19569147</ref> <ref>PMID:20080550</ref> <ref>PMID:22137895</ref>	+	[[https://www.uniprot.org/uniprot/ISPH_ECOLI ISPH_ECOLI]] Converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Is also involved in penicillin tolerance and control of the stringent response. Seems to directly or indirectly interact with RelA to maintain it in an inactive form during normal growth.<ref>PMID:19569147</ref> <ref>PMID:20080550</ref> <ref>PMID:22137895</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 23:

	==See Also==		==See Also==
-	*[[4-hydroxy-3-methylbut-2-enyl diphosphate reductase\|4-hydroxy-3-methylbut-2-enyl diphosphate reductase]]	+	*[[4-hydroxy-3-methylbut-2-enyl diphosphate reductase 3D structures\|4-hydroxy-3-methylbut-2-enyl diphosphate reductase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 30:		Line 30:
	[[Category: 4-hydroxy-3-methylbut-2-enyl diphosphate reductase]]		[[Category: 4-hydroxy-3-methylbut-2-enyl diphosphate reductase]]
	[[Category: Ecoli]]		[[Category: Ecoli]]
		+	[[Category: Large Structures]]
	[[Category: Bacher, A]]		[[Category: Bacher, A]]
	[[Category: Eisenreich, W]]		[[Category: Eisenreich, W]]

OCA at 03:42, 5 August 2016

OCA — Fri, 05 Aug 2016 03:42:54 GMT

←Older revision		Revision as of 03:42, 5 August 2016
Line 1:		Line 1:
		+
	==IspH:HMBPP (substrate) structure of the E126D mutant==		==IspH:HMBPP (substrate) structure of the E126D mutant==
	<StructureSection load='3t0f' size='340' side='right' caption='[[3t0f]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='3t0f' size='340' side='right' caption='[[3t0f]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3t0f]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Escherichia_coli Escherichia coli~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T0F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T0F FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3t0f]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T0F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T0F FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=H6P:(2E)-4-HYDROXY-3-METHYLBUT-2-EN-1-YL+TRIHYDROGEN+DIPHOSPHATE'>H6P</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=H6P:(2E)-4-HYDROXY-3-METHYLBUT-2-EN-1-YL+TRIHYDROGEN+DIPHOSPHATE'>H6P</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3f7t\|3f7t]], [[3dnf\|3dnf]], [[3szl\|3szl]], [[3szo\|3szo]], [[3szu\|3szu]], [[3t0g\|3t0g]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3f7t\|3f7t]], [[3dnf\|3dnf]], [[3szl\|3szl]], [[3szo\|3szo]], [[3szu\|3szu]], [[3t0g\|3t0g]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ispH, lytB, yaaE, b0029, JW0027 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=~~562 Escherichia coli~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ispH, lytB, yaaE, b0029, JW0027 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-hydroxy-3-methylbut-2-enyl_diphosphate_reductase 4-hydroxy-3-methylbut-2-enyl diphosphate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.1.2 1.17.1.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-hydroxy-3-methylbut-2-enyl_diphosphate_reductase 4-hydroxy-3-methylbut-2-enyl diphosphate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.1.2 1.17.1.2] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3t0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t0f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3t0f RCSB], [http://www.ebi.ac.uk/pdbsum/3t0f PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3t0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t0f OCA], [http://pdbe.org/3t0f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3t0f RCSB], [http://www.ebi.ac.uk/pdbsum/3t0f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3t0f ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 3t0f" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[4-hydroxy-3-methylbut-2-enyl diphosphate reductase\|4-hydroxy-3-methylbut-2-enyl diphosphate reductase]]
	== References ==		== References ==
	<references/>		<references/>
Line 24:		Line 29:
	</StructureSection>		</StructureSection>
	[[Category: 4-hydroxy-3-methylbut-2-enyl diphosphate reductase]]		[[Category: 4-hydroxy-3-methylbut-2-enyl diphosphate reductase]]
-	[[Category: ~~Escherichia coli~~]]	+	[[Category: Ecoli]]
	[[Category: Bacher, A]]		[[Category: Bacher, A]]
	[[Category: Eisenreich, W]]		[[Category: Eisenreich, W]]

OCA at 15:34, 25 December 2014

OCA — Thu, 25 Dec 2014 15:34:16 GMT

←Older revision		Revision as of 15:34, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3t0f]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T0F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T0F FirstGlance]. <br>		<table><tr><td colspan='2'>[[3t0f]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T0F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T0F FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=H6P:(2E)-4-HYDROXY-3-METHYLBUT-2-EN-1-YL+TRIHYDROGEN+DIPHOSPHATE'>H6P</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=H6P:(2E)-4-HYDROXY-3-METHYLBUT-2-EN-1-YL+TRIHYDROGEN+DIPHOSPHATE'>H6P</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3f7t\|3f7t]], [[3dnf\|3dnf]], [[3szl\|3szl]], [[3szo\|3szo]], [[3szu\|3szu]], [[3t0g\|3t0g]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3f7t\|3f7t]], [[3dnf\|3dnf]], [[3szl\|3szl]], [[3szo\|3szo]], [[3szu\|3szu]], [[3t0g\|3t0g]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ispH, lytB, yaaE, b0029, JW0027 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ispH, lytB, yaaE, b0029, JW0027 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-hydroxy-3-methylbut-2-enyl_diphosphate_reductase 4-hydroxy-3-methylbut-2-enyl diphosphate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.1.2 1.17.1.2] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-hydroxy-3-methylbut-2-enyl_diphosphate_reductase 4-hydroxy-3-methylbut-2-enyl diphosphate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.1.2 1.17.1.2] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3t0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t0f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3t0f RCSB], [http://www.ebi.ac.uk/pdbsum/3t0f PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3t0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t0f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3t0f RCSB], [http://www.ebi.ac.uk/pdbsum/3t0f PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ISPH_ECOLI ISPH_ECOLI]] Converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Is also involved in penicillin tolerance and control of the stringent response. Seems to directly or indirectly interact with RelA to maintain it in an inactive form during normal growth.<ref>PMID:19569147</ref> <ref>PMID:20080550</ref> <ref>PMID:22137895</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 15:		Line 17:
	Crystal Structures of Mutant IspH Proteins Reveal a Rotation of the Substrate's Hydroxymethyl Group during Catalysis.,Span I, Grawert T, Bacher A, Eisenreich W, Groll M J Mol Biol. 2011 Nov 23. PMID:22137895<ref>PMID:22137895</ref>		Crystal Structures of Mutant IspH Proteins Reveal a Rotation of the Substrate's Hydroxymethyl Group during Catalysis.,Span I, Grawert T, Bacher A, Eisenreich W, Groll M J Mol Biol. 2011 Nov 23. PMID:22137895<ref>PMID:22137895</ref>

-	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, a database of the U.S. National Library of Medicine.<br>	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
	== References ==		== References ==
Line 23:		Line 25:
	[[Category: 4-hydroxy-3-methylbut-2-enyl diphosphate reductase]]		[[Category: 4-hydroxy-3-methylbut-2-enyl diphosphate reductase]]
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
-	[[Category: Bacher, A.]]	+	[[Category: Bacher, A]]
-	[[Category: Eisenreich, W.]]	+	[[Category: Eisenreich, W]]
-	[[Category: Graewert, T.]]	+	[[Category: Graewert, T]]
-	[[Category: Groll, M.]]	+	[[Category: Groll, M]]
-	[[Category: Span, I.]]	+	[[Category: Span, I]]
	[[Category: 3fe-4s iron-sulfur cluster]]		[[Category: 3fe-4s iron-sulfur cluster]]
	[[Category: Conserved cysteine]]		[[Category: Conserved cysteine]]

OCA at 06:40, 5 June 2014

OCA — Thu, 05 Jun 2014 06:40:37 GMT

←Older revision		Revision as of 06:40, 5 June 2014
Line 1:		Line 1:
-	[[~~Image:~~3t0f.~~png~~\|~~left~~\|~~200px~~]]	+	==IspH:HMBPP (substrate) structure of the E126D mutant==
		+	<StructureSection load='3t0f' size='340' side='right' caption='[[3t0f]], [[Resolution\|resolution]] 1.90Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3t0f]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T0F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T0F FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=H6P:(2E)-4-HYDROXY-3-METHYLBUT-2-EN-1-YL+TRIHYDROGEN+DIPHOSPHATE'>H6P</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3f7t\|3f7t]], [[3dnf\|3dnf]], [[3szl\|3szl]], [[3szo\|3szo]], [[3szu\|3szu]], [[3t0g\|3t0g]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ispH, lytB, yaaE, b0029, JW0027 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-hydroxy-3-methylbut-2-enyl_diphosphate_reductase 4-hydroxy-3-methylbut-2-enyl diphosphate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.1.2 1.17.1.2] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3t0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t0f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3t0f RCSB], [http://www.ebi.ac.uk/pdbsum/3t0f PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Isoprenoids derive from two universal precursors, isopentenyl diphosphate and dimethylallyl diphosphate, which in most human pathogens are synthesized in the deoxyxylulose phosphate pathway. The last step of this pathway is the conversion of (E)-1-hydroxy-2-methylbut-2-enyl-4-diphosphate into a mixture of isopentenyl diphosphate and dimethylallyl diphosphate catalyzed by the iron-sulfur protein IspH. The crystal structures reported here of the IspH mutant proteins T167C, E126D and E126Q reveal an alternative substrate conformation compared to the wild-type structure. Thus, the previously observed alkoxide complex decomposes, and the substrate's hydroxymethyl group rotates to interact with Glu126. The carboxyl group of Glu126 then donates a proton to the hydroxyl group to enable water elimination. The structural and functional studies provide further knowledge of the IspH reaction mechanism, which opens up new routes to inhibitor design against malaria and tuberculosis.

-	~~<!--~~	+	Crystal Structures of Mutant IspH Proteins Reveal a Rotation of the Substrate's Hydroxymethyl Group during Catalysis.,Span I, Grawert T, Bacher A, Eisenreich W, Groll M J Mol Biol. 2011 Nov 23. PMID:22137895<ref>PMID:22137895</ref>
-	~~The line below this paragraph, containing "STRUCTURE_3t0f", creates the "Structure Box" on~~ the ~~page~~.	+
-	~~You may change the PDB parameter (which sets the PDB file loaded into the applet)~~	+
-	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded)~~,	+
-	~~or leave the SCENE parameter empty for the default display~~.	+
-	-->	+
-	~~{{STRUCTURE_3t0f\| PDB=3t0f \| SCENE= }}~~	+

-	~~===IspH:HMBPP (substrate) structure~~ of the ~~E126D mutant===~~	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-		+	== References ==
-	~~<!--~~	+	<references/>
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_22137895}}, adds the Publication Abstract to the page~~	+	__TOC__
-	~~(as it appears on PubMed at http://www~~.~~pubmed~~.~~gov), where 22137895 is the PubMed ID number~~.	+	</StructureSection>
-	-->	+
-	~~{{ABSTRACT_PUBMED_22137895}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[3t0f]] is a 2 chain structure with sequence from [http:~~/~~/en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T0F OCA].~~	+
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:022137895<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: 4-hydroxy-3-methylbut-2-enyl diphosphate reductase]]		[[Category: 4-hydroxy-3-methylbut-2-enyl diphosphate reductase]]
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]

OCA at 05:38, 11 January 2012

OCA — Wed, 11 Jan 2012 05:38:32 GMT

←Older revision		Revision as of 05:38, 11 January 2012
Line 11:		Line 11:
	===IspH:HMBPP (substrate) structure of the E126D mutant===		===IspH:HMBPP (substrate) structure of the E126D mutant===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_22137895}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 22137895 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_22137895}}

	==About this Structure==		==About this Structure==
	[[3t0f]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T0F OCA].		[[3t0f]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T0F OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:022137895</ref><references group="xtra"/>
	[[Category: 4-hydroxy-3-methylbut-2-enyl diphosphate reductase]]		[[Category: 4-hydroxy-3-methylbut-2-enyl diphosphate reductase]]
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]

OCA at 08:10, 7 December 2011

OCA — Wed, 07 Dec 2011 08:10:14 GMT

←Older revision		Revision as of 08:10, 7 December 2011
Line 1:		Line 1:
-	[[Image:3t0f.~~jpg~~\|left\|200px]]	+	[[Image:3t0f.png\|left\|200px]]

	<!--		<!--

OCA at 06:27, 30 November 2011

OCA — Wed, 30 Nov 2011 06:27:41 GMT

←Older revision		Revision as of 06:27, 30 November 2011
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3t0f.jpg\|left\|200px]]

-	The ~~entry 3t0f~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3t0f", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3t0f\| PDB=3t0f \| SCENE= }}

-	~~Authors~~: ~~Span, I., Graewert, T., Bacher, A., Eisenreich, W., Groll, M.~~	+	===IspH:HMBPP (substrate) structure of the E126D mutant===

-	~~Description~~: ~~IspH~~:~~HMBPP (substrate) structure of the E126D mutant~~	+
		+	==About this Structure==
		+	[[3t0f]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T0F OCA].
		+	[[Category: 4-hydroxy-3-methylbut-2-enyl diphosphate reductase]]
		+	[[Category: Escherichia coli]]
		+	[[Category: Bacher, A.]]
		+	[[Category: Eisenreich, W.]]
		+	[[Category: Graewert, T.]]
		+	[[Category: Groll, M.]]
		+	[[Category: Span, I.]]
		+	[[Category: 3fe-4s iron-sulfur cluster]]
		+	[[Category: Conserved cysteine]]
		+	[[Category: Ipp and dmapp production final step]]
		+	[[Category: Low activity]]
		+	[[Category: Non-mevalonate pathway]]
		+	[[Category: Oxidoreductase]]
		+	[[Category: Substrate hmbpp]]

OCA at 08:38, 30 October 2011

OCA — Sun, 30 Oct 2011 08:38:03 GMT

←Older revision		Revision as of 08:38, 30 October 2011
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3t0f is ON HOLD	+	The entry 3t0f is ON HOLD until Paper Publication

	Authors: Span, I., Graewert, T., Bacher, A., Eisenreich, W., Groll, M.		Authors: Span, I., Graewert, T., Bacher, A., Eisenreich, W., Groll, M.

	Description: IspH:HMBPP (substrate) structure of the E126D mutant		Description: IspH:HMBPP (substrate) structure of the E126D mutant

OCA at 06:01, 14 September 2011

OCA — Wed, 14 Sep 2011 06:01:13 GMT

←Older revision		Revision as of 06:01, 14 September 2011
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3t0f is ON HOLD ~~until Paper Publication~~	+	The entry 3t0f is ON HOLD

	Authors: Span, I., Graewert, T., Bacher, A., Eisenreich, W., Groll, M.		Authors: Span, I., Graewert, T., Bacher, A., Eisenreich, W., Groll, M.

	Description: IspH:HMBPP (substrate) structure of the E126D mutant		Description: IspH:HMBPP (substrate) structure of the E126D mutant