1b58: Difference between revisions

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[[Image:1b58.gif|left|200px]]
[[Image:1b58.gif|left|200px]]


{{Structure
<!--
|PDB= 1b58 |SIZE=350|CAPTION= <scene name='initialview01'>1b58</scene>, resolution 1.8&Aring;
The line below this paragraph, containing "STRUCTURE_1b58", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
|LIGAND= <scene name='pdbligand=IUM:URANYL+(VI)+ION'>IUM</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|GENE= OPPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=602 Salmonella typhimurium])
-->
|DOMAIN=
{{STRUCTURE_1b58| PDB=1b58 |  SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b58 OCA], [http://www.ebi.ac.uk/pdbsum/1b58 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b58 RCSB]</span>
}}


'''OLIGO-PEPTIDE BINDING PROTEIN (OPPA) COMPLEXED WITH KYK'''
'''OLIGO-PEPTIDE BINDING PROTEIN (OPPA) COMPLEXED WITH KYK'''
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[[Category: Tame, J R.H.]]
[[Category: Tame, J R.H.]]
[[Category: Wilkinson, A J.]]
[[Category: Wilkinson, A J.]]
[[Category: complex (peptide transport/peptide)]]
[[Category: Peptide transport]]
[[Category: peptide transport]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:05:17 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:53:55 2008''

Revision as of 11:05, 2 May 2008

File:1b58.gif

Template:STRUCTURE 1b58

OLIGO-PEPTIDE BINDING PROTEIN (OPPA) COMPLEXED WITH KYK


OverviewOverview

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.

About this StructureAbout this Structure

1B58 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 Fri May 2 11:05:17 2008

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