2v7t - Revision history

OCA at 15:09, 13 December 2023

OCA — Wed, 13 Dec 2023 15:09:03 GMT

←Older revision		Revision as of 15:09, 13 December 2023
Line 3:		Line 3:
	<StructureSection load='2v7t' size='340' side='right'caption='[[2v7t]], [[Resolution\|resolution]] 2.15Å' scene=''>		<StructureSection load='2v7t' size='340' side='right'caption='[[2v7t]], [[Resolution\|resolution]] 2.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2v7t]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"streptomyces_cattleya"_kahan_et_al._1979 "streptomyces~~ cattleya~~" kahan et al. 1979~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V7T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V7T FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2v7t]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_cattleya Streptomyces cattleya]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V7T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V7T FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>~~, ~~<scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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]] 2.15Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[1rqp\|1rqp]], [[2c2w\|2c2w]], [[2c4u\|2c4u]], [[2cbx\|2cbx]], [[2cc2\|2cc2]], [[1rqr\|1rqr]], [[2c4t\|2c4t]], [[2c5b\|2c5b]], [[2c5h\|2c5h]], [[2v7u\|2v7u]], [[2v7v\|2v7v]], [[2v7w\|2v7w]], [[2v7x\|2v7x]]~~</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Adenosyl~~-~~fluoride_synthase Adenosyl~~-~~fluoride synthase], with EC number [https://www.brenda~~-~~enzymes.info/php/result_flat.php4?ecno=2.5.1.63 2.5.1.63]~~ </~~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=2v7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v7t OCA], [https://pdbe.org/2v7t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v7t RCSB], [https://www.ebi.ac.uk/pdbsum/2v7t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v7t 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=2v7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v7t OCA], [https://pdbe.org/2v7t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v7t RCSB], [https://www.ebi.ac.uk/pdbsum/2v7t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v7t ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/FLA_STRCT FLA_STRCT] Involved in the biosynthesis of fluorometabolites. Catalyzes the formation of a C-F bond by combining S-adenosyl-L-methionine (SAM) and fluoride to generate 5'-fluoro-5'-deoxyadenosine (5'-FDA) and L-methionine. It can also use 2'-deoxyadenosine in place of adenosine as substrate.<ref>PMID:12860396</ref> <ref>PMID:14765200</ref> <ref>PMID:16370017</ref> <ref>PMID:16604208</ref> <ref>PMID:16720268</ref> <ref>PMID:17985882</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Streptomyces cattleya kahan et al. 1979]]
-	[[Category: Adenosyl-fluoride synthase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Hagan, D O~~]]	+	[[Category: Streptomyces cattleya]]
-	[[Category: Naismith~~, J H~~]]	+	[[Category: Naismith JH]]
-	[[Category: ~~Zhu, X~~]]	+	[[Category: O'Hagan D]]
-	[[Category: ~~Biosynthetic protein]]~~	+	[[Category: Zhu X]]
-	~~[[Category: Mechanism of fluorination]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 20:58, 20 October 2021

OCA — Wed, 20 Oct 2021 20:58:39 GMT

←Older revision		Revision as of 20:58, 20 October 2021
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	<StructureSection load='2v7t' size='340' side='right'caption='[[2v7t]], [[Resolution\|resolution]] 2.15Å' scene=''>		<StructureSection load='2v7t' size='340' side='right'caption='[[2v7t]], [[Resolution\|resolution]] 2.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2v7t]] is a 3 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"streptomyces_cattleya"_kahan_et_al._1979 "streptomyces cattleya" kahan et al. 1979]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V7T OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2V7T FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2v7t]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/"streptomyces_cattleya"_kahan_et_al._1979 "streptomyces cattleya" kahan et al. 1979]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V7T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V7T FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1rqp\|1rqp]], [[2c2w\|2c2w]], [[2c4u\|2c4u]], [[2cbx\|2cbx]], [[2cc2\|2cc2]], [[1rqr\|1rqr]], [[2c4t\|2c4t]], [[2c5b\|2c5b]], [[2c5h\|2c5h]], [[2v7u\|2v7u]], [[2v7v\|2v7v]], [[2v7w\|2v7w]], [[2v7x\|2v7x]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1rqp\|1rqp]], [[2c2w\|2c2w]], [[2c4u\|2c4u]], [[2cbx\|2cbx]], [[2cc2\|2cc2]], [[1rqr\|1rqr]], [[2c4t\|2c4t]], [[2c5b\|2c5b]], [[2c5h\|2c5h]], [[2v7u\|2v7u]], [[2v7v\|2v7v]], [[2v7w\|2v7w]], [[2v7x\|2v7x]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Adenosyl-fluoride_synthase Adenosyl-fluoride synthase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.63 2.5.1.63] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Adenosyl-fluoride_synthase Adenosyl-fluoride synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.63 2.5.1.63] </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=2v7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v7t OCA], [~~http~~://pdbe.org/2v7t PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2v7t RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2v7t PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2v7t 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=2v7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v7t OCA], [https://pdbe.org/2v7t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v7t RCSB], [https://www.ebi.ac.uk/pdbsum/2v7t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v7t ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==

OCA at 12:58, 1 January 2020

OCA — Wed, 01 Jan 2020 12:58:10 GMT

←Older revision		Revision as of 12:58, 1 January 2020
Line 1:		Line 1:

	==X-ray crystal structure of 5'-fluorodeoxyadenosine synthase s158g mutant complexed with s-adenosyl-l-homocysteine and chloride ion==		==X-ray crystal structure of 5'-fluorodeoxyadenosine synthase s158g mutant complexed with s-adenosyl-l-homocysteine and chloride ion==
-	<StructureSection load='2v7t' size='340' side='right' caption='[[2v7t]], [[Resolution\|resolution]] 2.15Å' scene=''>	+	<StructureSection load='2v7t' size='340' side='right'caption='[[2v7t]], [[Resolution\|resolution]] 2.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2v7t]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"streptomyces_cattleya"_kahan_et_al._1979 "streptomyces cattleya" kahan et al. 1979]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V7T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V7T FirstGlance]. <br>		<table><tr><td colspan='2'>[[2v7t]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"streptomyces_cattleya"_kahan_et_al._1979 "streptomyces cattleya" kahan et al. 1979]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V7T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V7T FirstGlance]. <br>
Line 34:		Line 34:
	[[Category: Streptomyces cattleya kahan et al. 1979]]		[[Category: Streptomyces cattleya kahan et al. 1979]]
	[[Category: Adenosyl-fluoride synthase]]		[[Category: Adenosyl-fluoride synthase]]
		+	[[Category: Large Structures]]
	[[Category: Hagan, D O]]		[[Category: Hagan, D O]]
	[[Category: Naismith, J H]]		[[Category: Naismith, J H]]

OCA at 06:53, 28 March 2018

OCA — Wed, 28 Mar 2018 06:53:14 GMT

←Older revision		Revision as of 06:53, 28 March 2018
Line 1:		Line 1:
-	==X-~~RAY CRYSTAL STRUCTURE OF~~ 5'-~~FLUORODEOXYADENOSINE SYNTHASE S158G MUTANT COMPLEXED WITH S~~-~~ADENOSYL~~-L-~~HOMOCYSTEINE AND CHLORIDE ION~~==	+
		+	==X-ray crystal structure of 5'-fluorodeoxyadenosine synthase s158g mutant complexed with s-adenosyl-l-homocysteine and chloride ion==
	<StructureSection load='2v7t' size='340' side='right' caption='[[2v7t]], [[Resolution\|resolution]] 2.15Å' scene=''>		<StructureSection load='2v7t' size='340' side='right' caption='[[2v7t]], [[Resolution\|resolution]] 2.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1rqp\|1rqp]], [[2c2w\|2c2w]], [[2c4u\|2c4u]], [[2cbx\|2cbx]], [[2cc2\|2cc2]], [[1rqr\|1rqr]], [[2c4t\|2c4t]], [[2c5b\|2c5b]], [[2c5h\|2c5h]], [[2v7u\|2v7u]], [[2v7v\|2v7v]], [[2v7w\|2v7w]], [[2v7x\|2v7x]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1rqp\|1rqp]], [[2c2w\|2c2w]], [[2c4u\|2c4u]], [[2cbx\|2cbx]], [[2cc2\|2cc2]], [[1rqr\|1rqr]], [[2c4t\|2c4t]], [[2c5b\|2c5b]], [[2c5h\|2c5h]], [[2v7u\|2v7u]], [[2v7v\|2v7v]], [[2v7w\|2v7w]], [[2v7x\|2v7x]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosyl-fluoride_synthase Adenosyl-fluoride synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.63 2.5.1.63] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosyl-fluoride_synthase Adenosyl-fluoride synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.63 2.5.1.63] </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=2v7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v7t OCA], [http://pdbe.org/2v7t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2v7t RCSB], [http://www.ebi.ac.uk/pdbsum/2v7t 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=2v7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v7t OCA], [http://pdbe.org/2v7t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2v7t RCSB], [http://www.ebi.ac.uk/pdbsum/2v7t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2v7t ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v7/2v7t_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v7/2v7t_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 07:35, 8 February 2016

OCA — Mon, 08 Feb 2016 07:35:57 GMT

←Older revision		Revision as of 07:35, 8 February 2016
Line 2:		Line 2:
	<StructureSection load='2v7t' size='340' side='right' caption='[[2v7t]], [[Resolution\|resolution]] 2.15Å' scene=''>		<StructureSection load='2v7t' size='340' side='right' caption='[[2v7t]], [[Resolution\|resolution]] 2.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2v7t]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Streptomyces_cattleya Streptomyces~~ cattleya]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V7T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V7T FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2v7t]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"streptomyces_cattleya"_kahan_et_al._1979 "streptomyces cattleya" kahan et al. 1979]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V7T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V7T FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1rqp\|1rqp]], [[2c2w\|2c2w]], [[2c4u\|2c4u]], [[2cbx\|2cbx]], [[2cc2\|2cc2]], [[1rqr\|1rqr]], [[2c4t\|2c4t]], [[2c5b\|2c5b]], [[2c5h\|2c5h]], [[2v7u\|2v7u]], [[2v7v\|2v7v]], [[2v7w\|2v7w]], [[2v7x\|2v7x]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1rqp\|1rqp]], [[2c2w\|2c2w]], [[2c4u\|2c4u]], [[2cbx\|2cbx]], [[2cc2\|2cc2]], [[1rqr\|1rqr]], [[2c4t\|2c4t]], [[2c5b\|2c5b]], [[2c5h\|2c5h]], [[2v7u\|2v7u]], [[2v7v\|2v7v]], [[2v7w\|2v7w]], [[2v7x\|2v7x]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosyl-fluoride_synthase Adenosyl-fluoride synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.63 2.5.1.63] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosyl-fluoride_synthase Adenosyl-fluoride synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.63 2.5.1.63] </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=2v7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v7t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2v7t RCSB], [http://www.ebi.ac.uk/pdbsum/2v7t 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=2v7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v7t OCA], [http://pdbe.org/2v7t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2v7t RCSB], [http://www.ebi.ac.uk/pdbsum/2v7t PDBsum]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 16:		Line 16:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2v7t ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 26:		Line 26:
	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 2v7t" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Streptomyces cattleya kahan et al. 1979]]
	[[Category: Adenosyl-fluoride synthase]]		[[Category: Adenosyl-fluoride synthase]]
-	[[Category: Streptomyces cattleya]]
	[[Category: Hagan, D O]]		[[Category: Hagan, D O]]
	[[Category: Naismith, J H]]		[[Category: Naismith, J H]]

OCA at 17:33, 19 January 2015

OCA — Mon, 19 Jan 2015 17:33:09 GMT

←Older revision		Revision as of 17:33, 19 January 2015
Line 32:		Line 32:
	[[Category: Adenosyl-fluoride synthase]]		[[Category: Adenosyl-fluoride synthase]]
	[[Category: Streptomyces cattleya]]		[[Category: Streptomyces cattleya]]
-	[[Category: Hagan, D O.]]	+	[[Category: Hagan, D O]]
-	[[Category: Naismith, J H.]]	+	[[Category: Naismith, J H]]
-	[[Category: Zhu, X.]]	+	[[Category: Zhu, X]]
	[[Category: Biosynthetic protein]]		[[Category: Biosynthetic protein]]
	[[Category: Mechanism of fluorination]]		[[Category: Mechanism of fluorination]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 06:32, 10 October 2014

OCA — Fri, 10 Oct 2014 06:32:24 GMT

←Older revision		Revision as of 06:32, 10 October 2014
Line 2:		Line 2:
	<StructureSection load='2v7t' size='340' side='right' caption='[[2v7t]], [[Resolution\|resolution]] 2.15Å' scene=''>		<StructureSection load='2v7t' size='340' side='right' caption='[[2v7t]], [[Resolution\|resolution]] 2.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2v7t]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_cattleya Streptomyces cattleya]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V7T OCA]. <br>	+	<table><tr><td colspan='2'>[[2v7t]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_cattleya Streptomyces cattleya]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V7T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V7T FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1rqp\|1rqp]], [[2c2w\|2c2w]], [[2c4u\|2c4u]], [[2cbx\|2cbx]], [[2cc2\|2cc2]], [[1rqr\|1rqr]], [[2c4t\|2c4t]], [[2c5b\|2c5b]], [[2c5h\|2c5h]], [[2v7u\|2v7u]], [[2v7v\|2v7v]], [[2v7w\|2v7w]], [[2v7x\|2v7x]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1rqp\|1rqp]], [[2c2w\|2c2w]], [[2c4u\|2c4u]], [[2cbx\|2cbx]], [[2cc2\|2cc2]], [[1rqr\|1rqr]], [[2c4t\|2c4t]], [[2c5b\|2c5b]], [[2c5h\|2c5h]], [[2v7u\|2v7u]], [[2v7v\|2v7v]], [[2v7w\|2v7w]], [[2v7x\|2v7x]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/~~Glucokinase Glucokinase~~], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosyl-fluoride_synthase Adenosyl-fluoride synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.63 2.5.1.63] </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=2v7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v7t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2v7t RCSB], [http://www.ebi.ac.uk/pdbsum/2v7t 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=2v7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v7t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2v7t RCSB], [http://www.ebi.ac.uk/pdbsum/2v7t PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 24:		Line 24:
	Mechanism of enzymatic fluorination in Streptomyces cattleya.,Zhu X, Robinson DA, McEwan AR, O'Hagan D, Naismith JH J Am Chem Soc. 2007 Nov 28;129(47):14597-604. Epub 2007 Nov 7. PMID:17985882<ref>PMID:17985882</ref>		Mechanism of enzymatic fluorination in Streptomyces cattleya.,Zhu X, Robinson DA, McEwan AR, O'Hagan D, Naismith JH J Am Chem Soc. 2007 Nov 28;129(47):14597-604. Epub 2007 Nov 7. PMID:17985882<ref>PMID:17985882</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 ==

OCA at 08:40, 7 May 2014

OCA — Wed, 07 May 2014 08:40:47 GMT

←Older revision		Revision as of 08:40, 7 May 2014
Line 1:		Line 1:
-	[[~~Image:~~2v7t.~~png~~\|~~left~~\|200px]]	+	==X-RAY CRYSTAL STRUCTURE OF 5'-FLUORODEOXYADENOSINE SYNTHASE S158G MUTANT COMPLEXED WITH S-ADENOSYL-L-HOMOCYSTEINE AND CHLORIDE ION==
		+	<StructureSection load='2v7t' size='340' side='right' caption='[[2v7t]], [[Resolution\|resolution]] 2.15Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2v7t]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_cattleya Streptomyces cattleya]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V7T OCA]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1rqp\|1rqp]], [[2c2w\|2c2w]], [[2c4u\|2c4u]], [[2cbx\|2cbx]], [[2cc2\|2cc2]], [[1rqr\|1rqr]], [[2c4t\|2c4t]], [[2c5b\|2c5b]], [[2c5h\|2c5h]], [[2v7u\|2v7u]], [[2v7v\|2v7v]], [[2v7w\|2v7w]], [[2v7x\|2v7x]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </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=2v7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v7t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2v7t RCSB], [http://www.ebi.ac.uk/pdbsum/2v7t PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v7/2v7t_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Recently a fluorination enzyme was identified and isolated from Streptomyces cattleya, as the first committed step on the metabolic pathway to the fluorinated metabolites, fluoroacetate and 4-fluorothreonine. This enzyme, 5'-fluoro-5'-deoxy adenosine synthetase (FDAS), has been shown to catalyze C-F bond formation by nucleophilic attack of fluoride ion to S-adenosyl-l-methionine (SAM) with the concomitant displacement of l-methionine to generate 5'-fluoro-5'-deoxy adenosine (5'-FDA). Although the structures of FDAS bound to both SAM and products have been solved, the molecular mechanism remained to be elucidated. We now report site-directed mutagenesis studies, structural analyses, and isothermal calorimetry (ITC) experiments. The data establish the key residues required for catalysis and the order of substrate binding. Fluoride ion is not readily distinguished from water by protein X-ray crystallography; however, using chloride ion (also a substrate) with a mutant of low activity has enabled the halide ion to be located in nonproductive co-complexes with SAH and SAM. The kinetic data suggest the positively charged sulfur of SAM is a key requirement in stabilizing the transition state. We propose a molecular mechanism for FDAS in which fluoride weakly associates with the enzyme exchanging two water molecules for protein ligation. The binding of SAM expels remaining water associated with fluoride ion and traps the ion in a pocket positioned to react with SAM, generating l-methionine and 5'-FDA. l-methionine then dissociates from the enzyme followed by 5'-FDA.

-	~~<!--~~	+	Mechanism of enzymatic fluorination in Streptomyces cattleya.,Zhu X, Robinson DA, McEwan AR, O'Hagan D, Naismith JH J Am Chem Soc. 2007 Nov 28;129(47):14597-604. Epub 2007 Nov 7. PMID:17985882<ref>PMID:17985882</ref>
-	~~The line below this paragraph~~, ~~containing "STRUCTURE_2v7t"~~, ~~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_2v7t\| PDB=2v7t \| SCENE= }}~~	+

-	~~===X-RAY CRYSTAL STRUCTURE OF 5'-FLUORODEOXYADENOSINE SYNTHASE S158G MUTANT COMPLEXED WITH S-ADENOSYL-L-HOMOCYSTEINE AND CHLORIDE ION===~~	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-		+	== References ==
-	~~<!--~~	+	<references/>
-	~~The line below this paragraph~~, ~~{{ABSTRACT_PUBMED_17985882}}, adds~~ the ~~Publication Abstract to the page~~	+	__TOC__
-	~~(as it appears on PubMed at http://www~~.~~pubmed~~.~~gov), where 17985882 is the PubMed ID number~~.	+	</StructureSection>
-	-->	+
-	~~{{ABSTRACT_PUBMED_17985882}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[2v7t]] is a 3 chain structure with sequence from [http:~~/~~/en.wikipedia.org/wiki/Streptomyces_cattleya Streptomyces cattleya]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V7T OCA].~~	+
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:017985882<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Adenosyl-fluoride synthase]]		[[Category: Adenosyl-fluoride synthase]]
	[[Category: Streptomyces cattleya]]		[[Category: Streptomyces cattleya]]

OCA: Protected "2v7t" [edit=sysop:move=sysop]

OCA — Wed, 24 Aug 2011 05:34:44 GMT

Protected "2v7t" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:34, 24 August 2011

OCA at 05:34, 24 August 2011

OCA — Wed, 24 Aug 2011 05:34:42 GMT

←Older revision		Revision as of 05:34, 24 August 2011
Line 1:		Line 1:
-	{{Seed}}
	[[Image:2v7t.png\|left\|200px]]		[[Image:2v7t.png\|left\|200px]]

Line 20:		Line 19:

	==About this Structure==		==About this Structure==
-	~~2V7T~~ is a 3 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Streptomyces_cattleya Streptomyces cattleya]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V7T OCA].	+	[[2v7t]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_cattleya Streptomyces cattleya]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V7T OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~17985882~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:017985882</ref><references group="xtra"/>
	[[Category: Adenosyl-fluoride synthase]]		[[Category: Adenosyl-fluoride synthase]]
	[[Category: Streptomyces cattleya]]		[[Category: Streptomyces cattleya]]
Line 32:		Line 31:
	[[Category: Mechanism of fluorination]]		[[Category: Mechanism of fluorination]]
	[[Category: Transferase]]		[[Category: Transferase]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 20:14:40 2009''