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 <StructureSection load='5yqw' size='340' side='right' caption='[[5yqw]], [[Resolution|resolution]] 1.36&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5yqw]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YQW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YQW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5yqw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibh1 Vibh1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YQW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YQW FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CBS:DI(N-ACETYL-D-GLUCOSAMINE)'>CBS</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=P4G:1-ETHOXY-2-(2-ETHOXYETHOXY)ETHANE'>P4G</scene></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VME_26970 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=673519 VIBH1])</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=5yqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yqw OCA], [http://pdbe.org/5yqw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yqw RCSB], [http://www.ebi.ac.uk/pdbsum/5yqw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yqw ProSAT]</span></td></tr>
 </table>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
-This research describes four X-ray structures of Vibrio harveyi chitinase A and its catalytically inactive mutant (E315M) in the presence and absence of substrates. The overall structure of chitinase A is that of a typical family-18 glycosyl hydrolase comprising three distinct domains: (i) the amino-terminal chitin-binding domain; (ii) the main catalytic (alpha/beta)(8) TIM-barrel domain; and (iii) the small (alpha+beta) insertion domain. The catalytic cleft of chitinase A has a long, deep groove, which contains six chitooligosaccharide ring-binding subsites (-4)(-3)(-2)(-1)(+1)(+2). The binding cleft of the ligand-free E315M is partially blocked by the C-terminal (His)(6)-tag. Structures of E315M-chitooligosaccharide complexes display a linear conformation of pentaNAG, but a bent conformation of hexaNAG. Analysis of the final 2F(o)-F(c) omit map of E315M-NAG6 reveals the existence of the linear conformation of the hexaNAG at a lower occupancy with respect to the bent conformation. These crystallographic data provide evidence that the interacting sugars undergo conformational changes prior to hydrolysis by the wild-type enzyme.
+Periplasmic solute-binding proteins in bacteria are involved in the active transport of nutrients into the cytoplasm. In marine bacteria of the genus Vibrio, a chitooligosaccharide-binding protein (CBP) is thought to be the major solute-binding protein controlling the rate of chitin uptake in these bacteria. However, the molecular mechanism of the CBP involvement in chitin metabolism has not been elucidated. Here, we report the structure and function of a recombinant chitooligosaccharide-binding protein from Vibrio harveyi, namely VhCBP, expressed in Escherichia coli Isothermal titration calorimetry revealed that VhCBP strongly binds shorter chitooligosaccharides ((GlcNAc) n , where n = 2, 3, and 4) with affinities that are considerably greater than those for glycoside hydrolase family 18 and 19 chitinases but does not bind longer ones, including insoluble chitin polysaccharides. We also found that VhCBP comprises two domains with flexible linkers and that the domain-domain interface forms the sugar-binding cleft, which is not long extended but forms a small cavity. (GlcNAc)2 bound to this cavity, apparently triggering a closed conformation of VhCBP. Trp-363 and Trp-513, which stack against the two individual GlcNAc rings, likely make a major contribution to the high affinity of VhCBP for (GlcNAc)2 The strong chitobiose binding, followed by the conformational change of VhCBP, may facilitate its interaction with an active-transport system in the inner membrane of Vibrio species.
-Crystal structures of Vibrio harveyi chitinase A complexed with chitooligosaccharides: implications for the catalytic mechanism.,Songsiriritthigul C, Pantoom S, Aguda AH, Robinson RC, Suginta W J Struct Biol. 2008 Jun;162(3):491-9. Epub 2008 Mar 26. PMID:18467126<ref>PMID:18467126</ref>
+Structure and function of a novel periplasmic chitooligosaccharide-binding protein from marine Vibrio bacteria.,Suginta W, Sritho N, Ranok A, Bulmer DM, Kitaoku Y, van den Berg B, Fukamizo T J Biol Chem. 2018 Apr 6;293(14):5150-5159. doi: 10.1074/jbc.RA117.001012. Epub, 2018 Feb 14. PMID:29444825<ref>PMID:29444825</ref>
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
 <div class="pdbe-citations 5yqw" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[ABC transporter|ABC transporter]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Vibh1]]
 [[Category: Berg, B van den]]
 [[Category: Bulmer, D M]]