1gvt
From Proteopedia
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| - | [[Image:1gvt.gif|left|200px]] | + | [[Image:1gvt.gif|left|200px]] |
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| - | '''ENDOTHIAPEPSIN COMPLEX WITH CP-80,794''' | + | {{Structure |
| + | |PDB= 1gvt |SIZE=350|CAPTION= <scene name='initialview01'>1gvt</scene>, resolution 0.98Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Endothiapepsin Endothiapepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.22 3.4.23.22] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''ENDOTHIAPEPSIN COMPLEX WITH CP-80,794''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GVT is a [ | + | 1GVT is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Cryphonectria_parasitica Cryphonectria parasitica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GVT OCA]. |
==Reference== | ==Reference== | ||
| - | Five atomic resolution structures of endothiapepsin inhibitor complexes: implications for the aspartic proteinase mechanism., Coates L, Erskine PT, Crump MP, Wood SP, Cooper JB, J Mol Biol. 2002 May 17;318(5):1405-15. PMID:[http:// | + | Five atomic resolution structures of endothiapepsin inhibitor complexes: implications for the aspartic proteinase mechanism., Coates L, Erskine PT, Crump MP, Wood SP, Cooper JB, J Mol Biol. 2002 May 17;318(5):1405-15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12083527 12083527] |
[[Category: Cryphonectria parasitica]] | [[Category: Cryphonectria parasitica]] | ||
[[Category: Endothiapepsin]] | [[Category: Endothiapepsin]] | ||
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[[Category: tetrahedral intermediate]] | [[Category: tetrahedral intermediate]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:28:37 2008'' |
Revision as of 09:28, 20 March 2008
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| , resolution 0.98Å | |||||||
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| Ligands: | |||||||
| Activity: | Endothiapepsin, with EC number 3.4.23.22 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ENDOTHIAPEPSIN COMPLEX WITH CP-80,794
Overview
Endothiapepsin is derived from the fungus Endothia parasitica and is a member of the aspartic proteinase class of enzymes. This class of enzyme is comprised of two structurally similar lobes, each lobe contributing an aspartic acid residue to form a catalytic dyad that acts to cleave the substrate peptide bond. The three-dimensional structures of endothiapepsin bound to five transition state analogue inhibitors (H189, H256, CP-80,794, PD-129,541 and PD-130,328) have been solved at atomic resolution allowing full anisotropic modelling of each complex. The active sites of the five structures have been studied with a view to studying the catalytic mechanism of the aspartic proteinases by locating the active site protons by carboxyl bond length differences and electron density analysis. In the CP-80,794 structure there is excellent electron density for the hydrogen on the inhibitory statine hydroxyl group which forms a hydrogen bond with the inner oxygen of Asp32. The location of this proton has implications for the catalytic mechanism of the aspartic proteinases as it is consistent with the proposed mechanism in which Asp32 is the negatively charged aspartate. A number of short hydrogen bonds (approximately 2.6 A) with ESD values of around 0.01 A that may have a role in catalysis have been identified within the active site of each structure; the lengths of these bonds have been confirmed using NMR techniques. The possibility and implications of low barrier hydrogen bonds in the active site are considered.
About this Structure
1GVT is a Protein complex structure of sequences from Cryphonectria parasitica. Full crystallographic information is available from OCA.
Reference
Five atomic resolution structures of endothiapepsin inhibitor complexes: implications for the aspartic proteinase mechanism., Coates L, Erskine PT, Crump MP, Wood SP, Cooper JB, J Mol Biol. 2002 May 17;318(5):1405-15. PMID:12083527
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