1b4z: Difference between revisions
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|PDB= 1b4z |SIZE=350|CAPTION= <scene name='initialview01'>1b4z</scene>, resolution 1.75Å | |PDB= 1b4z |SIZE=350|CAPTION= <scene name='initialview01'>1b4z</scene>, resolution 1.75Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=IUM:URANYL+(VI)+ION'>IUM</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= OPPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=602 Salmonella typhimurium]) | |GENE= OPPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=602 Salmonella typhimurium]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b4z OCA], [http://www.ebi.ac.uk/pdbsum/1b4z PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b4z RCSB]</span> | |||
}} | }} | ||
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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: complex (peptide transport/peptide)]] | ||
[[Category: peptide transport]] | [[Category: peptide transport]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:53:45 2008'' | ||
Revision as of 18:53, 30 March 2008
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| , resolution 1.75Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | OPPA (Salmonella typhimurium) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OLIGO-PEPTIDE BINDING PROTEIN (OPPA) COMPLEXED WITH KDK
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
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
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