1fno
From Proteopedia
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| - | [[Image:1fno.gif|left|200px]] | + | [[Image:1fno.gif|left|200px]] |
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| - | '''PEPTIDASE T (TRIPEPTIDASE)''' | + | {{Structure |
| + | |PDB= 1fno |SIZE=350|CAPTION= <scene name='initialview01'>1fno</scene>, resolution 2.4Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''PEPTIDASE T (TRIPEPTIDASE)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1FNO is a [ | + | 1FNO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FNO OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of peptidase T from Salmonella typhimurium., Hakansson K, Miller CG, Eur J Biochem. 2002 Jan;269(2):443-50. PMID:[http:// | + | Structure of peptidase T from Salmonella typhimurium., Hakansson K, Miller CG, Eur J Biochem. 2002 Jan;269(2):443-50. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11856302 11856302] |
[[Category: Salmonella typhimurium]] | [[Category: Salmonella typhimurium]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: zinc]] | [[Category: zinc]] | ||
| - | ''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 11:11:31 2008'' |
Revision as of 09:11, 20 March 2008
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| , resolution 2.4Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PEPTIDASE T (TRIPEPTIDASE)
Overview
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 Structure
1FNO is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.
Reference
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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