1xlh - Revision history

OCA at 08:51, 14 February 2024

OCA — Wed, 14 Feb 2024 08:51:18 GMT

←Older revision		Revision as of 08:51, 14 February 2024
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	<StructureSection load='1xlh' size='340' side='right'caption='[[1xlh]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='1xlh' size='340' side='right'caption='[[1xlh]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1xlh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Arts7 Arts7~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XLH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XLH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1xlh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arthrobacter_sp._NRRL_B3728 Arthrobacter sp. NRRL B3728]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XLH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XLH FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=AL:ALUMINUM+ION'>AL</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]] 2.5Å</td></tr>
-	<tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"><~~span class~~='~~plainlinks~~'>~~[https://en.wikipedia.org/wiki/Xylose_isomerase Xylose isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.5 5.3.1.5]~~ </~~span~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AL:ALUMINUM+ION'>AL</scene></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=1xlh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xlh OCA], [https://pdbe.org/1xlh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xlh RCSB], [https://www.ebi.ac.uk/pdbsum/1xlh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xlh 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=1xlh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xlh OCA], [https://pdbe.org/1xlh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xlh RCSB], [https://www.ebi.ac.uk/pdbsum/1xlh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xlh ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/XYLA_ARTS7 XYLA_ARTS7]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</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=1xlh 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=1xlh ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The active site and mechanism of D-xylose isomerase have been probed by determination of the crystal structures of the enzyme bound to various substrates, inhibitors and cations. Ring-opening is an obligatory first step of the reaction and is believed to be the rate-determining step for the aldose to ketose conversion. The structure of a complex with a cyclic thio-glucose has been determined and it is concluded that this is an analogue of the Michaelis complex. At -10 degrees C substrates in crystals are observed in the extended chain form. The absence of an appropriately situated base for either the cyclic or extended chain forms from the substrate binding site indicates that the isomerisation does not take place by an enediol or enediolate mechanism. Binding of a trivalent cation places an additional charge at the active site, producing a substrate complex that is analogous to a possible transition state. Of the two binding sites for divalent cations, [1] is permanently occupied under catalytic conditions and is co-ordinated to four carboxylate groups. In the absence of substrate it is exposed to solvent, and in the Michaelis complex analogue, site [1] is octahedrally coordinated, with ligands to O-3 and O-4 of the thiopyranose. In the complex with an open-chain substrate it remains octahedrally co-ordinated, with ligands to O-2 and O-4. Binding at a second cation site [2] is also necessary for catalysis and this site is believed to bind Co2+ more strongly than site [1]. This site is octahedrally co-ordinated to three carboxylate groups (bidentate co-ordination to one of them), an imidazole and a solvent molecule. It is proposed that during the hydride shift the C-O-1 and C-O-2 bonds of the substrate are polarized by the close approach of the site [2] cation. In the transition-state analogue this cation is observed at a site [2'], 1.0 A from site [2] and about 2.7 A from O-1 and O-2 of the substrate. It is likely that co-ordination of the cation to O-1 and O-2 would be concomitant with ionisation of the sugar hydroxyl group. The polarisation of C-O-1 and C-O-2 is assisted by the co-ordination of O-2 to cation [1] and O-1 to a lysine side-chain.(ABSTRACT TRUNCATED AT 400 WORDS)
-
-	Mechanism for aldose-ketose interconversion by D-xylose isomerase involving ring opening followed by a 1,2-hydride shift.,Collyer CA, Henrick K, Blow DM J Mol Biol. 1990 Mar 5;212(1):211-35. PMID:2319597<ref>PMID:2319597</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1xlh" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
-	*[[D-xylose isomerase\|D-xylose isomerase]]	+	*[[D-xylose isomerase 3D structures\|D-xylose isomerase 3D structures]]
-	~~== References ==~~	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Arts7~~]]	+	[[Category: Arthrobacter sp. NRRL B3728]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Xylose isomerase]]~~	+	[[Category: Blow DM]]
-	[[Category: Blow~~, D M~~]]	+	[[Category: Collyer CA]]
-	[[Category: Collyer~~, C A~~]]	+	[[Category: Henrick K]]
-	[[Category: Henrick, K]]	+

OCA at 06:31, 6 October 2021

OCA — Wed, 06 Oct 2021 06:31:48 GMT

←Older revision		Revision as of 06:31, 6 October 2021
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	<StructureSection load='1xlh' size='340' side='right'caption='[[1xlh]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='1xlh' size='340' side='right'caption='[[1xlh]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1xlh]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Arts7 Arts7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XLH OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1XLH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1xlh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arts7 Arts7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XLH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XLH FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AL:ALUMINUM+ION'>AL</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AL:ALUMINUM+ION'>AL</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Xylose_isomerase Xylose isomerase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.5 5.3.1.5] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Xylose_isomerase Xylose isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.5 5.3.1.5] </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=1xlh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xlh OCA], [~~http~~://pdbe.org/1xlh PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1xlh RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1xlh PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1xlh 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=1xlh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xlh OCA], [https://pdbe.org/1xlh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xlh RCSB], [https://www.ebi.ac.uk/pdbsum/1xlh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xlh ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==

OCA at 11:43, 4 December 2019

OCA — Wed, 04 Dec 2019 11:43:51 GMT

←Older revision		Revision as of 11:43, 4 December 2019
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	==MECHANISM FOR ALDOSE-KETOSE INTERCONVERSION BY D-XYLOSE ISOMERASE INVOLVING RING OPENING FOLLOWED BY A 1,2-HYDRIDE SHIFT==		==MECHANISM FOR ALDOSE-KETOSE INTERCONVERSION BY D-XYLOSE ISOMERASE INVOLVING RING OPENING FOLLOWED BY A 1,2-HYDRIDE SHIFT==
-	<StructureSection load='1xlh' size='340' side='right' caption='[[1xlh]], [[Resolution\|resolution]] 2.50Å' scene=''>	+	<StructureSection load='1xlh' size='340' side='right'caption='[[1xlh]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1xlh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arts7 Arts7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XLH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XLH FirstGlance]. <br>		<table><tr><td colspan='2'>[[1xlh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arts7 Arts7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XLH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XLH FirstGlance]. <br>
Line 12:		Line 12:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xl/1xlh_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xl/1xlh_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>
Line 27:		Line 27:
	</div>		</div>
	<div class="pdbe-citations 1xlh" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1xlh" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[D-xylose isomerase\|D-xylose isomerase]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Arts7]]		[[Category: Arts7]]
		+	[[Category: Large Structures]]
	[[Category: Xylose isomerase]]		[[Category: Xylose isomerase]]
	[[Category: Blow, D M]]		[[Category: Blow, D M]]
	[[Category: Collyer, C A]]		[[Category: Collyer, C A]]
	[[Category: Henrick, K]]		[[Category: Henrick, K]]

OCA at 07:01, 29 November 2017

OCA — Wed, 29 Nov 2017 07:01:33 GMT

←Older revision		Revision as of 07:01, 29 November 2017
Line 1:		Line 1:
		+
	==MECHANISM FOR ALDOSE-KETOSE INTERCONVERSION BY D-XYLOSE ISOMERASE INVOLVING RING OPENING FOLLOWED BY A 1,2-HYDRIDE SHIFT==		==MECHANISM FOR ALDOSE-KETOSE INTERCONVERSION BY D-XYLOSE ISOMERASE INVOLVING RING OPENING FOLLOWED BY A 1,2-HYDRIDE SHIFT==
	<StructureSection load='1xlh' size='340' side='right' caption='[[1xlh]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='1xlh' size='340' side='right' caption='[[1xlh]], [[Resolution\|resolution]] 2.50Å' scene=''>
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	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AL:ALUMINUM+ION'>AL</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AL:ALUMINUM+ION'>AL</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Xylose_isomerase Xylose isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.5 5.3.1.5] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Xylose_isomerase Xylose isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.5 5.3.1.5] </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=1xlh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xlh OCA], [http://pdbe.org/1xlh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xlh RCSB], [http://www.ebi.ac.uk/pdbsum/1xlh 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=1xlh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xlh OCA], [http://pdbe.org/1xlh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xlh RCSB], [http://www.ebi.ac.uk/pdbsum/1xlh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xlh ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
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	</div>		</div>
	<div class="pdbe-citations 1xlh" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1xlh" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[D-xylose isomerase\|D-xylose isomerase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 13:45, 8 February 2016

OCA — Mon, 08 Feb 2016 13:45:28 GMT

←Older revision		Revision as of 13:45, 8 February 2016
Line 15:		Line 15:
	<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=1xlh ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 12:08, 10 September 2015

OCA — Thu, 10 Sep 2015 12:08:25 GMT

←Older revision		Revision as of 12:08, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1xlh' size='340' side='right' caption='[[1xlh]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='1xlh' size='340' side='right' caption='[[1xlh]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1xlh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Arthrobacter_sp. Arthrobacter sp.~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XLH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XLH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1xlh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arts7 Arts7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XLH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XLH FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AL:ALUMINUM+ION'>AL</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AL:ALUMINUM+ION'>AL</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Xylose_isomerase Xylose isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.5 5.3.1.5] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Xylose_isomerase Xylose isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.5 5.3.1.5] </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=1xlh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xlh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1xlh RCSB], [http://www.ebi.ac.uk/pdbsum/1xlh 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=1xlh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xlh OCA], [http://pdbe.org/1xlh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xlh RCSB], [http://www.ebi.ac.uk/pdbsum/1xlh PDBsum]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 25:		Line 25:
	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 1xlh" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 32:		Line 33:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Arthrobacter sp~~]]	+	[[Category: Arts7]]
	[[Category: Xylose isomerase]]		[[Category: Xylose isomerase]]
	[[Category: Blow, D M]]		[[Category: Blow, D M]]
	[[Category: Collyer, C A]]		[[Category: Collyer, C A]]
	[[Category: Henrick, K]]		[[Category: Henrick, K]]

OCA at 13:04, 6 January 2015

OCA — Tue, 06 Jan 2015 13:04:10 GMT

←Older revision		Revision as of 13:04, 6 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1xlh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arthrobacter_sp. Arthrobacter sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XLH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XLH FirstGlance]. <br>		<table><tr><td colspan='2'>[[1xlh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arthrobacter_sp. Arthrobacter sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XLH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XLH FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AL:ALUMINUM+ION'>AL</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AL:ALUMINUM+ION'>AL</scene></td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Xylose_isomerase Xylose isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.5 5.3.1.5] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Xylose_isomerase Xylose isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.5 5.3.1.5] </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=1xlh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xlh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1xlh RCSB], [http://www.ebi.ac.uk/pdbsum/1xlh 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=1xlh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xlh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1xlh RCSB], [http://www.ebi.ac.uk/pdbsum/1xlh 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 32:		Line 32:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Arthrobacter sp.]]	+	[[Category: Arthrobacter sp]]
	[[Category: Xylose isomerase]]		[[Category: Xylose isomerase]]
-	[[Category: Blow, D M.]]	+	[[Category: Blow, D M]]
-	[[Category: Collyer, C A.]]	+	[[Category: Collyer, C A]]
-	[[Category: Henrick, K.]]	+	[[Category: Henrick, K]]

OCA at 19:42, 29 September 2014

OCA — Mon, 29 Sep 2014 19:42:18 GMT

←Older revision		Revision as of 19:42, 29 September 2014
Line 1:		Line 1:
-	[[~~Image~~:1xlh.~~png\|left~~\|200px]]	+	==MECHANISM FOR ALDOSE-KETOSE INTERCONVERSION BY D-XYLOSE ISOMERASE INVOLVING RING OPENING FOLLOWED BY A 1,2-HYDRIDE SHIFT==
		+	<StructureSection load='1xlh' size='340' side='right' caption='[[1xlh]], [[Resolution\|resolution]] 2.50Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1xlh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arthrobacter_sp. Arthrobacter sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XLH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XLH FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AL:ALUMINUM+ION'>AL</scene><br>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Xylose_isomerase Xylose isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.5 5.3.1.5] </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=1xlh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xlh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1xlh RCSB], [http://www.ebi.ac.uk/pdbsum/1xlh 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/xl/1xlh_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 ==
		+	The active site and mechanism of D-xylose isomerase have been probed by determination of the crystal structures of the enzyme bound to various substrates, inhibitors and cations. Ring-opening is an obligatory first step of the reaction and is believed to be the rate-determining step for the aldose to ketose conversion. The structure of a complex with a cyclic thio-glucose has been determined and it is concluded that this is an analogue of the Michaelis complex. At -10 degrees C substrates in crystals are observed in the extended chain form. The absence of an appropriately situated base for either the cyclic or extended chain forms from the substrate binding site indicates that the isomerisation does not take place by an enediol or enediolate mechanism. Binding of a trivalent cation places an additional charge at the active site, producing a substrate complex that is analogous to a possible transition state. Of the two binding sites for divalent cations, [1] is permanently occupied under catalytic conditions and is co-ordinated to four carboxylate groups. In the absence of substrate it is exposed to solvent, and in the Michaelis complex analogue, site [1] is octahedrally coordinated, with ligands to O-3 and O-4 of the thiopyranose. In the complex with an open-chain substrate it remains octahedrally co-ordinated, with ligands to O-2 and O-4. Binding at a second cation site [2] is also necessary for catalysis and this site is believed to bind Co2+ more strongly than site [1]. This site is octahedrally co-ordinated to three carboxylate groups (bidentate co-ordination to one of them), an imidazole and a solvent molecule. It is proposed that during the hydride shift the C-O-1 and C-O-2 bonds of the substrate are polarized by the close approach of the site [2] cation. In the transition-state analogue this cation is observed at a site [2'], 1.0 A from site [2] and about 2.7 A from O-1 and O-2 of the substrate. It is likely that co-ordination of the cation to O-1 and O-2 would be concomitant with ionisation of the sugar hydroxyl group. The polarisation of C-O-1 and C-O-2 is assisted by the co-ordination of O-2 to cation [1] and O-1 to a lysine side-chain.(ABSTRACT TRUNCATED AT 400 WORDS)

-	~~{{STRUCTURE_1xlh\| PDB=1xlh \| SCENE= }}~~	+	Mechanism for aldose-ketose interconversion by D-xylose isomerase involving ring opening followed by a 1,2-hydride shift.,Collyer CA, Henrick K, Blow DM J Mol Biol. 1990 Mar 5;212(1):211-35. PMID:2319597<ref>PMID:2319597</ref>

-	~~===MECHANISM FOR ALDOSE-KETOSE INTERCONVERSION BY D-XYLOSE ISOMERASE INVOLVING RING OPENING FOLLOWED BY A 1~~,~~2-HYDRIDE SHIFT===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_2319597}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1xlh]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Arthrobacter_sp~~. ~~Arthrobacter sp.]. Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1XLH OCA].~~	+

	==See Also==		==See Also==
	*[[D-xylose isomerase\|D-xylose isomerase]]		*[[D-xylose isomerase\|D-xylose isomerase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:002319597<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Arthrobacter sp.]]		[[Category: Arthrobacter sp.]]
	[[Category: Xylose isomerase]]		[[Category: Xylose isomerase]]

OCA: Protected "1xlh" [edit=sysop:move=sysop]

OCA — Sat, 05 Jan 2013 12:58:32 GMT

Protected "1xlh" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:58, 5 January 2013

OCA at 12:58, 5 January 2013

OCA — Sat, 05 Jan 2013 12:58:29 GMT

←Older revision		Revision as of 12:58, 5 January 2013
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1xlh.png\|left\|200px]]		[[Image:1xlh.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1xlh", 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.
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	{{STRUCTURE_1xlh\| PDB=1xlh \| SCENE= }}		{{STRUCTURE_1xlh\| PDB=1xlh \| SCENE= }}

	===MECHANISM FOR ALDOSE-KETOSE INTERCONVERSION BY D-XYLOSE ISOMERASE INVOLVING RING OPENING FOLLOWED BY A 1,2-HYDRIDE SHIFT===		===MECHANISM FOR ALDOSE-KETOSE INTERCONVERSION BY D-XYLOSE ISOMERASE INVOLVING RING OPENING FOLLOWED BY A 1,2-HYDRIDE SHIFT===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_2319597}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 2319597 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_2319597}}		{{ABSTRACT_PUBMED_2319597}}

	==About this Structure==		==About this Structure==
-	~~1XLH~~ is a 2 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Arthrobacter_sp. Arthrobacter sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XLH OCA].	+	[[1xlh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arthrobacter_sp. Arthrobacter sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XLH OCA].
		+
		+	==See Also==
		+	*[[D-xylose isomerase\|D-xylose isomerase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~2319597~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:002319597</ref><references group="xtra"/>
	[[Category: Arthrobacter sp.]]		[[Category: Arthrobacter sp.]]
	[[Category: Xylose isomerase]]		[[Category: Xylose isomerase]]
Line 29:		Line 20:
	[[Category: Collyer, C A.]]		[[Category: Collyer, C A.]]
	[[Category: Henrick, K.]]		[[Category: Henrick, K.]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 22:59:21 2009''