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| | ==Crystal structure of Pseudomonas stutzeri L-rhamnose isomerase mutant H101N in complex with D-allopyranose== | | ==Crystal structure of Pseudomonas stutzeri L-rhamnose isomerase mutant H101N in complex with D-allopyranose== |
| - | <StructureSection load='4gjj' size='340' side='right' caption='[[4gjj]], [[Resolution|resolution]] 2.38Å' scene=''> | + | <StructureSection load='4gjj' size='340' side='right'caption='[[4gjj]], [[Resolution|resolution]] 2.38Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4gjj]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"achromobacter_sewerinii"_bergey_et_al._1923 "achromobacter sewerinii" bergey et al. 1923]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GJJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GJJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4gjj]] 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=4GJJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GJJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AFD:ALPHA-D-ALLOPYRANOSE'>AFD</scene>, <scene name='pdbligand=AOS:D-ALLOSE'>AOS</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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]] 2.38Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2hcv|2hcv]], [[2i57|2i57]], [[4gji|4gji]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AFD:ALPHA-D-ALLOPYRANOSE'>AFD</scene>, <scene name='pdbligand=AOS:D-ALLOSE'>AOS</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">L-RhI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=316 "Achromobacter sewerinii" Bergey et al. 1923])</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=4gjj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gjj OCA], [https://pdbe.org/4gjj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gjj RCSB], [https://www.ebi.ac.uk/pdbsum/4gjj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gjj ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-rhamnose_isomerase L-rhamnose isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.14 5.3.1.14] </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=4gjj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gjj OCA], [http://pdbe.org/4gjj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gjj RCSB], [http://www.ebi.ac.uk/pdbsum/4gjj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gjj ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q75WH8_PSEST Q75WH8_PSEST] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4gjj" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4gjj" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[L-rhamnose isomerase|L-rhamnose isomerase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Achromobacter sewerinii bergey et al. 1923]] | + | [[Category: Large Structures]] |
| - | [[Category: L-rhamnose isomerase]] | + | [[Category: Pseudomonas stutzeri]] |
| - | [[Category: Kamitori, S]] | + | [[Category: Kamitori S]] |
| - | [[Category: Yoshida, H]] | + | [[Category: Yoshida H]] |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Metal binding]]
| + | |
| - | [[Category: Sugar binding]]
| + | |
| - | [[Category: Tim barrel]]
| + | |
| Structural highlights
Function
Q75WH8_PSEST
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yoshida H, Yoshihara A, Teraoka M, Yamashita S, Izumori K, Kamitori S. 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. FEBS Open Bio. 2012 Dec 7;3:35-40. doi: 10.1016/j.fob.2012.11.008. Print 2013. PMID:23772372 doi:http://dx.doi.org/10.1016/j.fob.2012.11.008
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