2d49: Difference between revisions
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<StructureSection load='2d49' size='340' side='right' caption='[[2d49]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | <StructureSection load='2d49' size='340' side='right' caption='[[2d49]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2d49]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2d49]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_griseus"_krainsky_1914 "actinomyces griseus" krainsky 1914]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D49 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2D49 FirstGlance]. <br> | ||
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chitinase Chitinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.14 3.2.1.14] </span></td></tr> | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chitinase Chitinase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2d49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d49 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2d49 RCSB], [http://www.ebi.ac.uk/pdbsum/2d49 PDBsum]</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=2d49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d49 OCA], [http://pdbe.org/2d49 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2d49 RCSB], [http://www.ebi.ac.uk/pdbsum/2d49 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2d49" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Actinomyces griseus krainsky 1914]] | |||
[[Category: Chitinase]] | [[Category: Chitinase]] | ||
[[Category: Akagi, K]] | [[Category: Akagi, K]] | ||
[[Category: Akutsu, H]] | [[Category: Akutsu, H]] | ||
Revision as of 14:21, 10 September 2015
Solution structure of the Chitin-Binding Domain of Streptomyces griseus Chitinase CSolution structure of the Chitin-Binding Domain of Streptomyces griseus Chitinase C
Structural highlights
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 PubMedChitinase C from Streptomyces griseus HUT6037 was discovered as the first bacterial chitinase in family 19 other than chitinases found in higher plants. Chitinase C comprises two domains: a chitin-binding domain (ChBD(ChiC)) for attachment to chitin and a chitin-catalytic domain for digesting chitin. The structure of ChBD(ChiC) was determined by means of 13C-, 15N-, and 1H-resonance nuclear magnetic resonance (NMR) spectroscopy. The conformation of its backbone comprised two beta-sheets composed of two and three antiparallel beta-strands, respectively, this being very similar to the backbone conformations of the cellulose-binding domain of endoglucanase Z from Erwinia chrysanthemi (CBD(EGZ)) and the chitin-binding domain of chitinase A1 from Bacillus circulans WL-12 (ChBD(ChiA1)). The interaction between ChBD(ChiC) and hexa-N-acetyl-chitohexaose was monitored through chemical shift perturbations, which showed that ChBD(ChiC) interacted with the substrate through two aromatic rings exposed to the solvent as CBD(EGZ) interacts with cellulose through three characteristic aromatic rings. Comparison of the conformations of ChBD(ChiA1), ChBD(ChiC), and other typical chitin- and cellulose-binding domains, which have three solvent-exposed aromatic residues responsible for binding to polysaccharides, has suggested that they have adopted versatile binding site conformations depending on the substrates, with almost the same backbone conformations being retained. Identification of the substrate interaction region of the chitin-binding domain of Streptomyces griseus chitinase C.,Akagi K, Watanabe J, Hara M, Kezuka Y, Chikaishi E, Yamaguchi T, Akutsu H, Nonaka T, Watanabe T, Ikegami T J Biochem. 2006 Mar;139(3):483-93. PMID:16567413[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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