1lok: Difference between revisions

Revision as of 21:35, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1lok.png

Template:STRUCTURE 1lok

The 1.20 Angstrom Resolution Crystal Structure of the Aminopeptidase from Aeromonas proteolytica Complexed with Tris: A Tale of Buffer InhibitionThe 1.20 Angstrom Resolution Crystal Structure of the Aminopeptidase from Aeromonas proteolytica Complexed with Tris: A Tale of Buffer Inhibition

Template:ABSTRACT PUBMED 12176384

About this StructureAbout this Structure

1LOK is a Single protein structure of sequence from Vibrio proteolyticus. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Wed Jul 2 21:35:56 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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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'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12176384}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12176384 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12176384}}
 ==About this Structure==
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 [[Category: Metalloenzyme]]
 [[Category: Tri]]
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