1fno: Difference between revisions
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|PDB= 1fno |SIZE=350|CAPTION= <scene name='initialview01'>1fno</scene>, resolution 2.4Å | |PDB= 1fno |SIZE=350|CAPTION= <scene name='initialview01'>1fno</scene>, resolution 2.4Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fno OCA], [http://www.ebi.ac.uk/pdbsum/1fno PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fno RCSB]</span> | |||
}} | }} | ||
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[[Category: Hakansson, K.]] | [[Category: Hakansson, K.]] | ||
[[Category: Miller, C G.]] | [[Category: Miller, C G.]] | ||
[[Category: metallo peptidase]] | [[Category: metallo peptidase]] | ||
[[Category: protease]] | [[Category: protease]] | ||
[[Category: zinc]] | [[Category: zinc]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:26:34 2008'' | ||
Revision as of 20:26, 30 March 2008
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| , resolution 2.4Å | |||||||
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| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PEPTIDASE T (TRIPEPTIDASE)
OverviewOverview
The structure of peptidase T, or tripeptidase, was determined by multiple wavelength anomalous dispersion (MAD) methodology and refined to 2.4 A resolution. Peptidase T comprises two domains; a catalytic domain with an active site containing two metal ions, and a smaller domain formed through a long insertion into the catalytic domain. The two metal ions, presumably zinc, are separated by 3.3 A, and are coordinated by five carboxylate and histidine ligands. The molecular surface of the active site is negatively charged. Peptidase T has the same basic fold as carboxypeptidase G2. When the structures of the two enzymes are superimposed, a number of homologous residues, not evident from the sequence alone, could be identified. Comparison of the active sites of peptidase T, carboxypeptidase G2, Aeromonas proteolytica aminopeptidase, carboxypeptidase A and leucine aminopeptidase reveals a common structural framework with interesting similarities and differences in the active sites and in the zinc coordination. A putative binding site for the C-terminal end of the tripeptide substrate was found at a peptidase T specific fingerprint sequence motif.
About this StructureAbout this Structure
1FNO is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.
ReferenceReference
Structure of peptidase T from Salmonella typhimurium., Hakansson K, Miller CG, Eur J Biochem. 2002 Jan;269(2):443-50. PMID:11856302
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