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| - | [[Image:1euf.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1euf| PDB=1euf | SCENE= }} | | {{STRUCTURE_1euf| PDB=1euf | SCENE= }} |
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| - | '''BOVINE DUODENASE(NEW SERINE PROTEASE), CRYSTAL STRUCTURE'''
| + | ===BOVINE DUODENASE(NEW SERINE PROTEASE), CRYSTAL STRUCTURE=== |
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| - | ==Overview==
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| - | The three-dimensional structure of duodenase, a serine protease from bovine duodenum mucosa, has been determined at 2.4A resolution. The enzyme, which has both trypsin-like and chymotrypsin-like activities, most closely resembles human cathepsin G with which it shares 57% sequence identity and similar specificity. The catalytic Ser195 in duodenase adopts the energetically favored conformation typical of serine proteinases and unlike the strained state typical of lipase/esterases. Of several waters in the active site of duodenase, the one associated with Ser214 is found in all serine proteinases and most lipase/esterases. The conservation of the Ser214 residue in serine proteinase, its presence in the active site, and participation in a hydrogen water network involving the catalytic triad (His57, Asp107, and Ser195) argues for its having an important role in the mechanism of action. It may be referred to as a fourth member of the catalytic triad. Duodenase is one of a growing family of enzymes that possesses trypsin-like and chymotrypsin-like activity. Not long ago, these activities were considered to be mutually exclusive. Computer modeling reveals that the S1 subsite of duodenase has structural features compatible with effective accommodation of P1 residues typical of trypsin (Arg/Lys) and chymotrypsin (Tyr/Phe) substrates. The determination of structural features associated with functional variation in the enzyme family may permit design of enzymes with a specific ratio of trypsin and chymotrypsin activities. | + | The line below this paragraph, {{ABSTRACT_PUBMED_10944388}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10944388 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10944388}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Dual specificity]] | | [[Category: Dual specificity]] |
| | [[Category: Serine protease]] | | [[Category: Serine protease]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:31:42 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:00:18 2008'' |
Revision as of 23:00, 30 June 2008
Template:STRUCTURE 1euf
BOVINE DUODENASE(NEW SERINE PROTEASE), CRYSTAL STRUCTURE
Template:ABSTRACT PUBMED 10944388
About this Structure
1EUF is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Crystal structure of bovine duodenase, a serine protease, with dual trypsin and chymotrypsin-like specificities., Pletnev VZ, Zamolodchikova TS, Pangborn WA, Duax WL, Proteins. 2000 Oct 1;41(1):8-16. PMID:10944388
Page seeded by OCA on Tue Jul 1 02:00:18 2008
