1ecy
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Ecotin, a homodimeric protein composed of 142 residue subunits, is a novel | + | Ecotin, a homodimeric protein composed of 142 residue subunits, is a novel serine protease inhibitor present in Escherichia coli. Its thermostability and acid stability, as well as broad specificity toward proteases, make it an interesting protein for structural characterization. Its structure in the uncomplexed state, determined for two different crystalline environments, allows a structural comparison of the free inhibitor with that in complex with trypsin. Although there is no gross structural rearrangement of ecotin when binding trypsin, the loops involved in binding trypsin show relatively large shifts in atomic positions. The inherent flexibility of the loops and the highly nonglobular shape are the two features essential for its inhibitory function. An insight into the understanding of the structural basis of thermostability and acid stability of ecotin is also provided by the present structure. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Shin, D | + | [[Category: Shin, D H.]] |
| - | [[Category: Suh, S | + | [[Category: Suh, S W.]] |
[[Category: GLC]] | [[Category: GLC]] | ||
[[Category: beta-sheet structure]] | [[Category: beta-sheet structure]] | ||
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[[Category: serine protease inhibitor]] | [[Category: serine protease inhibitor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:26:29 2008'' |
Revision as of 10:26, 21 February 2008
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PROTEASE INHIBITOR ECOTIN
Overview
Ecotin, a homodimeric protein composed of 142 residue subunits, is a novel serine protease inhibitor present in Escherichia coli. Its thermostability and acid stability, as well as broad specificity toward proteases, make it an interesting protein for structural characterization. Its structure in the uncomplexed state, determined for two different crystalline environments, allows a structural comparison of the free inhibitor with that in complex with trypsin. Although there is no gross structural rearrangement of ecotin when binding trypsin, the loops involved in binding trypsin show relatively large shifts in atomic positions. The inherent flexibility of the loops and the highly nonglobular shape are the two features essential for its inhibitory function. An insight into the understanding of the structural basis of thermostability and acid stability of ecotin is also provided by the present structure.
About this Structure
1ECY is a Single protein structure of sequence from Escherichia coli with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Crystal structure analyses of uncomplexed ecotin in two crystal forms: implications for its function and stability., Shin DH, Song HK, Seong IS, Lee CS, Chung CH, Suh SW, Protein Sci. 1996 Nov;5(11):2236-47. PMID:8931142
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