| pubmed-article:8564542 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8564542 | lifeskim:mentions | umls-concept:C0038420 | lld:lifeskim |
| pubmed-article:8564542 | lifeskim:mentions | umls-concept:C0043309 | lld:lifeskim |
| pubmed-article:8564542 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:8564542 | lifeskim:mentions | umls-concept:C0055320 | lld:lifeskim |
| pubmed-article:8564542 | lifeskim:mentions | umls-concept:C0718566 | lld:lifeskim |
| pubmed-article:8564542 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:8564542 | pubmed:dateCreated | 1996-3-6 | lld:pubmed |
| pubmed-article:8564542 | pubmed:abstractText | We report the 2.4 A X-ray crystal structure of a protein with chitosan endo-hydrolase activity isolated from Streptomyces N174. The structure was solved using phases acquired by SIRAS from a two-site methyl mercury derivative combined with solvent flattening and non-crystallographic two-fold symmetry averaging, and refined to an R-factor of 18.5%. The mostly alpha-helical fold reveals a structural core shared with several classes of lysozyme and barley endochitinase, in spite of a lack of shared sequence. Based on this structural similarity we postulate a putative active site, mechanism of action and mode of substrate recognition. It appears that Glu 22 acts as an acid and Asp 40 serves as a general base to activate a water molecule for an SN2 attack on the glycosidic bond. A series of amino-acid side chains and backbone carbonyl groups may bind the polycationic chitosan substrate in a deep electronegative binding cleft. | lld:pubmed |
| pubmed-article:8564542 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8564542 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8564542 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8564542 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8564542 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8564542 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8564542 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8564542 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:8564542 | pubmed:issn | 1072-8368 | lld:pubmed |
| pubmed-article:8564542 | pubmed:author | pubmed-author:BrzezinskaZZ | lld:pubmed |
| pubmed-article:8564542 | pubmed:author | pubmed-author:RobertusJ DJD | lld:pubmed |
| pubmed-article:8564542 | pubmed:author | pubmed-author:MonzingoA FAF | lld:pubmed |
| pubmed-article:8564542 | pubmed:author | pubmed-author:ErnstS RSR | lld:pubmed |
| pubmed-article:8564542 | pubmed:author | pubmed-author:MarcotteE MEM | lld:pubmed |
| pubmed-article:8564542 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8564542 | pubmed:volume | 3 | lld:pubmed |
| pubmed-article:8564542 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8564542 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8564542 | pubmed:pagination | 155-62 | lld:pubmed |
| pubmed-article:8564542 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:8564542 | pubmed:meshHeading | pubmed-meshheading:8564542-... | lld:pubmed |
| pubmed-article:8564542 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8564542 | pubmed:articleTitle | X-ray structure of an anti-fungal chitosanase from streptomyces N174. | lld:pubmed |
| pubmed-article:8564542 | pubmed:affiliation | Department of Chemistry and Biochemistry, University of Texas, Austin 78712, USA. | lld:pubmed |
| pubmed-article:8564542 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8564542 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8564542 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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