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3wz1

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<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=3wz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wz1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wz1 RCSB], [http://www.ebi.ac.uk/pdbsum/3wz1 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=3wz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wz1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wz1 RCSB], [http://www.ebi.ac.uk/pdbsum/3wz1 PDBsum]</span></td></tr>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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A deep-sea bacterium, Microbulbifer thermotolerans JAMB-A94, has a beta-agarase (MtAgaA) belonging to the glycoside hydrolase family (GH) 16. The optimal temperature of this bacterium for growth is 43-49 degrees C, and MtAgaA is stable at 60 degrees C, which is one of the most thermostable enzymes among GH16 beta-agarases. Here, we determined the catalytic domain structure of MtAgaA. MtAgaA consists of a beta-jelly roll fold, as observed in other GH16 enzymes. The structure of MtAgaA was most similar to two beta-agarases from Zobellia galactanivorans, ZgAgaA, and ZgAgaB. Although the catalytic cleft structure of MtAgaA was similar to ZgAgaA and ZgAgaB, residues at subsite -4 of MtAgaA were not conserved between them. Also, an alpha-helix, designated as alpha4', was uniquely located near the catalytic cleft of MtAgaA. A comparison of the structures of the three enzymes suggested that multiple factors, including increased numbers of arginine and proline residues, could contribute to the thermostability of MtAgaA.
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Crystal structure of the catalytic domain of a GH16 beta-agarase from a deep-sea bacterium, Microbulbifer thermotolerans JAMB-A94.,Takagi E, Hatada Y, Akita M, Ohta Y, Yokoi G, Miyazaki T, Nishikawa A, Tonozuka T Biosci Biotechnol Biochem. 2015 Apr;79(4):625-32. doi:, 10.1080/09168451.2014.988680. Epub 2014 Dec 6. PMID:25483365<ref>PMID:25483365</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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</StructureSection>
</StructureSection>

Revision as of 07:13, 22 April 2015

Catalytic domain of beta-agarase from Microbulbifer thermotolerans JAMB-A94

3wz1, resolution 1.60Å

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