1lok
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(New page: 200px<br /><applet load="1lok" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lok, resolution 1.20Å" /> '''The 1.20 Angstrom Re...)
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Revision as of 18:36, 20 November 2007
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The 1.20 Angstrom Resolution Crystal Structure of the Aminopeptidase from Aeromonas proteolytica Complexed with Tris: A Tale of Buffer Inhibition
Overview
The aminopeptidase from Aeromonas proteolytica (AAP) is a bridged, bimetallic enzyme that removes the N-terminal amino acid from a peptide, chain. To fully understand the metal roles in the reaction pathway of AAP, we have solved the 1.20 A resolution crystal structure of native AAP (PDB, ID = 1LOK). The high-quality electron density maps showed a single Tris, molecule chelated to the active site Zn(2+), alternate side chain, conformations for some side chains, a sodium ion that mediates a crystal, contact, a surface thiocyanate ion, and several potential hydrogen atoms., In addition, the high precision of the atomic positions has led to insight, into the protonation states of some of the active site amino acid side, chains.
About this Structure
1LOK is a Single protein structure of sequence from Vibrio proteolyticus with ZN, NA, SCN and TRS as ligands. Active as Bacterial leucyl aminopeptidase, with EC number 3.4.11.10 Full crystallographic information is available from OCA.
Reference
The 1.20 A resolution crystal structure of the aminopeptidase from Aeromonas proteolytica complexed with tris: a tale of buffer inhibition., Desmarais WT, Bienvenue DL, Bzymek KP, Holz RC, Petsko GA, Ringe D, Structure. 2002 Aug;10(8):1063-72. PMID:12176384
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