View source for 4gjj


==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]] 2.38&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.38&#8491;</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='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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q75WH8_PSEST Q75WH8_PSEST] 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:23772372</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4gjj" style="background-color:#fffaf0;"></div>

==See Also==
*[[L-rhamnose isomerase|L-rhamnose isomerase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas stutzeri]]
[[Category: Kamitori S]]
[[Category: Yoshida H]]