pubmed-article:19237546 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:19237546 | lifeskim:mentions | umls-concept:C0037949 | lld:lifeskim |
pubmed-article:19237546 | lifeskim:mentions | umls-concept:C0233820 | lld:lifeskim |
pubmed-article:19237546 | lifeskim:mentions | umls-concept:C0038592 | lld:lifeskim |
pubmed-article:19237546 | lifeskim:mentions | umls-concept:C0037633 | lld:lifeskim |
pubmed-article:19237546 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:19237546 | lifeskim:mentions | umls-concept:C1382100 | lld:lifeskim |
pubmed-article:19237546 | lifeskim:mentions | umls-concept:C1880371 | lld:lifeskim |
pubmed-article:19237546 | lifeskim:mentions | umls-concept:C0075284 | lld:lifeskim |
pubmed-article:19237546 | pubmed:issue | 16 | lld:pubmed |
pubmed-article:19237546 | pubmed:dateCreated | 2009-4-13 | lld:pubmed |
pubmed-article:19237546 | pubmed:abstractText | Streptococcal pyrogenic exotoxin B (SPE B) is a cysteine protease expressed by Streptococcus pyogenes. The D9N, G163S, G163S/A172S, and G239D mutant proteins were expressed to study the effect of the allelic variants on their protease activity. In contrast to other mutants, the G239D mutant was approximately 12-fold less active. The Gly-239 residue is located within the C-terminal S230-G239 region, which cannot be observed in the x-ray structure. The three-dimensional structure and backbone dynamics of the 28-kDa mature SPE B (mSPE B) were determined. Unlike the x-ray structure of the 40-kDa zymogen SPE B (proSPE B), we observed the interactions between the C-terminal loop and the active site residues in mSPE B. The structural differences between mSPE B and proSPE B were the conformation of the C-terminal loop and the orientation of the catalytic His-195 residue, suggesting that activation and inactivation of SPE B is involved in the His-195 side-chain rotation. Dynamics analysis of mSPE B and the mSPE B/inhibitor complexes showed that the catalytic and C-terminal loops were the most flexible regions with low order parameter values of 0.5 to 0.8 and exhibited the motion on the ps/ns timescale. These findings suggest that the flexible C-terminal loop of SPE B may play an important role in controlling the substrate binding, resulting in its broad substrate specificity. | lld:pubmed |
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pubmed-article:19237546 | pubmed:language | eng | lld:pubmed |
pubmed-article:19237546 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19237546 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:19237546 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19237546 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19237546 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:19237546 | pubmed:month | Apr | lld:pubmed |
pubmed-article:19237546 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:19237546 | pubmed:author | pubmed-author:LiuChing-Chua... | lld:pubmed |
pubmed-article:19237546 | pubmed:author | pubmed-author:WangChih-Chie... | lld:pubmed |
pubmed-article:19237546 | pubmed:author | pubmed-author:WuJiunn-JongJ... | lld:pubmed |
pubmed-article:19237546 | pubmed:author | pubmed-author:LimMing SMS | lld:pubmed |
pubmed-article:19237546 | pubmed:author | pubmed-author:ChenChun-Lian... | lld:pubmed |
pubmed-article:19237546 | pubmed:author | pubmed-author:LinYee-ShinYS | lld:pubmed |
pubmed-article:19237546 | pubmed:author | pubmed-author:HuangWenyaW | lld:pubmed |
pubmed-article:19237546 | pubmed:author | pubmed-author:ChuangWoei-Je... | lld:pubmed |
pubmed-article:19237546 | pubmed:author | pubmed-author:KuoChih-FengC... | lld:pubmed |
pubmed-article:19237546 | pubmed:author | pubmed-author:WangPei-JuPJ | lld:pubmed |
pubmed-article:19237546 | pubmed:author | pubmed-author:HoungHsiang-C... | lld:pubmed |
pubmed-article:19237546 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:19237546 | pubmed:day | 17 | lld:pubmed |
pubmed-article:19237546 | pubmed:volume | 284 | lld:pubmed |
pubmed-article:19237546 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:19237546 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:19237546 | pubmed:pagination | 10957-67 | lld:pubmed |
pubmed-article:19237546 | pubmed:dateRevised | 2010-9-22 | lld:pubmed |
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pubmed-article:19237546 | pubmed:year | 2009 | lld:pubmed |
pubmed-article:19237546 | pubmed:articleTitle | Solution structure and backbone dynamics of streptopain: insight into diverse substrate specificity. | lld:pubmed |
pubmed-article:19237546 | pubmed:affiliation | Departments of Biochemistry, Microbiology and Immunology, Medical Technology, and Pediatrics, National Cheng Kung University College of Medicine, 1 University Road, Tainan 701, Taiwan. | lld:pubmed |
pubmed-article:19237546 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:19237546 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:19237546 | lld:entrezgene |