1h0b | pdb_00001h0b

ENDOGLUCANASE CEL12A FROM RHODOTHERMUS MARINUS

spinqualitylabelsall models 1h0b, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1h0b is a 2 chain structure with sequence from Rhodothermus marinus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EPE Activity: Cellulase, with EC number 3.2.1.4 Resources: FirstGlance, OCA, RCSB, PDBsum 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 Cellulose is one of the most abundant polysaccharides in nature and microorganisms have developed a comprehensive system for enzymatic breakdown of this ubiquitous carbon source, a subject of much interest in the biotechnology industry. Rhodothermus marinus produces a hyperthermostable cellulase, with a temperature optimum of more than 90 degrees C, the structure of which is presented here to 1.8 A resolution. The enzyme has been classified into glycoside hydrolase family 12; this is the first structure of a thermophilic member of this family to have been solved. The beta-jelly roll fold observed has identical topology to those of the two mesophilic members of the family whose structures have been elucidated previously. A Hepes buffer molecule bound in the active site may have triggered a conformational change to an active configuration as the two catalytic residues Glu124 and Glu207, together with dependent residues, are observed in a conformation similar to that seen in the structure of Streptomyces lividans CelB2 complexed with an inhibitor. The structural similarity between this cellulase and the mesophilic enzymes serves to highlight features that may be responsible for its thermostability, chiefly an increase in ion pair number and the considerable stabilisation of a mobile region seen in S. lividans CelB2. Additional aromatic residues in the active site region may also contribute to the difference in thermophilicity. The structure of Rhodothermus marinus Cel12A, a highly thermostable family 12 endoglucanase, at 1.8 A resolution.,Crennell SJ, Hreggvidsson GO, Nordberg Karlsson E J Mol Biol. 2002 Jul 19;320(4):883-97. PMID:12095262 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glucanase

Proteopedia Page Contributors and Editors (what is this?)

OCA