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| | <StructureSection load='3b9e' size='340' side='right'caption='[[3b9e]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='3b9e' size='340' side='right'caption='[[3b9e]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3b9e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"achromobacter_harveyi"_johnson_and_shunk_1936 "achromobacter harveyi" johnson and shunk 1936]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B9E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B9E FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3b9e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_harveyi Vibrio harveyi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B9E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B9E FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ctn|1ctn]], [[3b8s|3b8s]], [[3b9a|3b9a]]</div></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]] 1.7Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CHIA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=669 "Achromobacter harveyi" Johnson and Shunk 1936])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Chitinase Chitinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.14 3.2.1.14] </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=3b9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b9e OCA], [https://pdbe.org/3b9e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b9e RCSB], [https://www.ebi.ac.uk/pdbsum/3b9e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b9e 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=3b9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b9e OCA], [https://pdbe.org/3b9e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b9e RCSB], [https://www.ebi.ac.uk/pdbsum/3b9e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b9e ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9AMP1_VIBHA Q9AMP1_VIBHA] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Achromobacter harveyi johnson and shunk 1936]] | |
| - | [[Category: Chitinase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Aguda, A H]] | + | [[Category: Vibrio harveyi]] |
| - | [[Category: Pantoom, S]] | + | [[Category: Aguda AH]] |
| - | [[Category: Robinson, R C]] | + | [[Category: Pantoom S]] |
| - | [[Category: Songsiriritthigul, C]] | + | [[Category: Robinson RC]] |
| - | [[Category: Suginta, W]] | + | [[Category: Songsiriritthigul C]] |
| - | [[Category: Glycosidase]]
| + | [[Category: Suginta W]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Tim-barrel]]
| + | |
| Structural highlights
Function
Q9AMP1_VIBHA
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Songsiriritthigul C, Pantoom S, Aguda AH, Robinson RC, Suginta W. Crystal structures of Vibrio harveyi chitinase A complexed with chitooligosaccharides: implications for the catalytic mechanism. J Struct Biol. 2008 Jun;162(3):491-9. Epub 2008 Mar 26. PMID:18467126 doi:10.1016/j.jsb.2008.03.008
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