1b4z: Difference between revisions

Revision as of 18:16, 30 June 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:1b4z.png

Template:STRUCTURE 1b4z

OLIGO-PEPTIDE BINDING PROTEIN (OPPA) COMPLEXED WITH KDKOLIGO-PEPTIDE BINDING PROTEIN (OPPA) COMPLEXED WITH KDK

Template:ABSTRACT PUBMED 10438628

About this StructureAbout this Structure

1B4Z is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.

ReferenceReference

Crystallographic and calorimetric analysis of peptide binding to OppA protein., Sleigh SH, Seavers PR, Wilkinson AJ, Ladbury JE, Tame JR, J Mol Biol. 1999 Aug 13;291(2):393-415. PMID:10438628

Page seeded by OCA on Mon Jun 30 18:16:39 2008

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-'''OLIGO-PEPTIDE BINDING PROTEIN (OPPA) COMPLEXED WITH KDK'''
+===OLIGO-PEPTIDE BINDING PROTEIN (OPPA) COMPLEXED WITH KDK===
-==Overview==
+<!--
-Isothermal titration calorimetry has been used to study the binding of 20 different peptides to the peptide binding protein OppA, and the crystal structures of the ligand complexes have been refined. This periplasmic binding protein, part of the oligopeptide permease system of Gram negative bacteria, has evolved to bind and enclose small peptides of widely varying sequences. The peptides used in this study have the sequence Lys-X-Lys, where X is any of the 20 commonly occurring amino acids. The various side-chains found at position 2 on the ligand fit into a hydrated pocket. The majority of side-chains are restrained to particular conformations within the pocket. Water molecules act as flexible adapters, matching the hydrogen-bonding requirements of the protein and ligand and shielding charges on the buried ligand. This use of water by OppA to broaden the repertoire of its binding site is not unique, but contrasts sharply with other proteins which use water to help bind ligands highly selectively. Predicting the thermodynamics of binding from the structure of the complexes is highly complicated by the influence of water on the system.
+The line below this paragraph, {{ABSTRACT_PUBMED_10438628}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10438628 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_10438628}}
 ==About this Structure==
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 [[Category: Wilkinson, A J.]]
 [[Category: Peptide transport]]
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