1m9u
From Proteopedia
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| - | + | {{STRUCTURE_1m9u| PDB=1m9u | SCENE= }} | |
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'''Crystal Structure of Earthworm Fibrinolytic Enzyme Component A from Eisenia fetida''' | '''Crystal Structure of Earthworm Fibrinolytic Enzyme Component A from Eisenia fetida''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1M9U is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Eisenia_fetida Eisenia fetida]. This structure supersedes the now removed PDB entry | + | 1M9U is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Eisenia_fetida Eisenia fetida]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ij7 1ij7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M9U OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Liang, D.]] | [[Category: Liang, D.]] | ||
[[Category: Tang, Y.]] | [[Category: Tang, Y.]] | ||
| - | [[Category: | + | [[Category: Fibrinolytic enzyme]] |
| - | [[Category: | + | [[Category: Hydrolase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:48:24 2008'' | |
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Revision as of 21:48, 2 May 2008
Crystal Structure of Earthworm Fibrinolytic Enzyme Component A from Eisenia fetida
Overview
Earthworm fibrinolytic enzyme component A (EFEa) from Eisenia fetida is a strong fibrinolytic enzyme that not only directly degrades fibrin, but also activates plasminogen. Proteolytic assays further revealed that it cleaved behind various P1 residue types. The crystal structure of EFEa was determined using the MIR method and refined to 2.3A resolution. The enzyme, showing the overall polypeptide fold of chymotrypsin-like serine proteases, possesses essential S1 specificity determinants characteristic of elastase. However, the beta strand at the west rim of the S1 specificity pocket is significantly elongated by a unique four-residue insertion (Ser-Ser-Gly-Leu) after Val217, which not only provides additional substrate hydrogen binding sites for distal P residues, but also causes extension of the S1 pocket at the south rim. The S2 subsite of the enzyme was partially occluded by the bulky side-chain of residue Tyr99. Structure-based inhibitor modeling demonstrated that EFEa's S1 specificity pocket was preferable for elastase-specific small hydrophobic P1 residues, while its accommodation of long and/or bulky P1 residues was also feasible if enhanced binding of the substrate and induced fit of the S1 pocket were achieved. EFEa is thereby endowed with relatively broad substrate specificity, including the dual fibrinolysis. The presence of Tyr99 at the S2 subsite indicates a preference for P2-Gly, while an induced fit of Tyr99 was also suggested for accommodation of bigger P2 residues. This structure is the first reported for an earthworm fibrinolytic enzyme component and serine protease originating from annelid worms.
About this Structure
1M9U is a Single protein structure of sequence from Eisenia fetida. This structure supersedes the now removed PDB entry 1ij7. Full crystallographic information is available from OCA.
Reference
Crystal structure of earthworm fibrinolytic enzyme component a: revealing the structural determinants of its dual fibrinolytic activity., Tang Y, Liang D, Jiang T, Zhang J, Gui L, Chang W, J Mol Biol. 2002 Aug 2;321(1):57-68. PMID:12139933 Page seeded by OCA on Sat May 3 00:48:24 2008
