4gji

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'''Unreleased structure'''
 
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The entry 4gji is ON HOLD
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==Crystal structure of Pseudomonas stutzeri L-rhamnose isomerase mutant H101N in complex with L-rhamnopyranose==
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<StructureSection load='4gji' size='340' side='right'caption='[[4gji]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4gji]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_stutzeri Pseudomonas stutzeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GJI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GJI FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=RAM:ALPHA-L-RHAMNOSE'>RAM</scene>, <scene name='pdbligand=RM4:6-DEOXY-BETA-L-MANNOPYRANOSE'>RM4</scene>, <scene name='pdbligand=RNS:L-RHAMNOSE'>RNS</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4gji FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gji OCA], [https://pdbe.org/4gji PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gji RCSB], [https://www.ebi.ac.uk/pdbsum/4gji PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gji ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q75WH8_PSEST Q75WH8_PSEST]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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l-Rhamnose isomerase (l-RhI) catalyzes the reversible isomerization of l-rhamnose to l-rhamnulose. Previously determined X-ray structures of l-RhI showed a hydride-shift mechanism for the isomerization of substrates in a linear form, but the mechanism for opening of the sugar-ring is still unclear. To elucidate this mechanism, we determined X-ray structures of a mutant l-RhI in complex with l-rhamnopyranose and d-allopyranose. Results suggest that a catalytic water molecule, which acts as an acid/base catalyst in the isomerization reaction, is likely to be involved in pyranose-ring opening, and that a newly found substrate sub-binding site in the vicinity of the catalytic site may recognize different anomers of substrates.
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Authors: Yoshida, H., Kamitori, S.
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Structure of l-rhamnose isomerase in complex with l-rhamnopyranose demonstrates the sugar-ring opening mechanism and the role of a substrate sub-binding site.,Yoshida H, Yoshihara A, Teraoka M, Yamashita S, Izumori K, Kamitori S FEBS Open Bio. 2012 Dec 7;3:35-40. doi: 10.1016/j.fob.2012.11.008. Print 2013. PMID:23772372<ref>PMID:23772372</ref>
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Description: Crystal structure of Pseudomonas stutzeri L-rhamnose isomerase mutant H101N in complex with L-rhamnopyranose
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4gji" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[L-rhamnose isomerase|L-rhamnose isomerase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Pseudomonas stutzeri]]
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[[Category: Kamitori S]]
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[[Category: Yoshida H]]

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Crystal structure of Pseudomonas stutzeri L-rhamnose isomerase mutant H101N in complex with L-rhamnopyranose

PDB ID 4gji

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