1b32

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "1b32" [edit=sysop:move=sysop])
Current revision (23:48, 20 November 2024) (edit) (undo)
 
(9 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1b32.png|left|200px]]
 
-
{{STRUCTURE_1b32| PDB=1b32 | SCENE= }}
+
==OLIGO-PEPTIDE BINDING PROTEIN (OPPA) COMPLEXED WITH KMK==
 +
<StructureSection load='1b32' size='340' side='right'caption='[[1b32]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1b32]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B32 FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=IUM:URANYL+(VI)+ION'>IUM</scene></td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1b32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b32 OCA], [https://pdbe.org/1b32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b32 RCSB], [https://www.ebi.ac.uk/pdbsum/1b32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b32 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/OPPA_SALTY OPPA_SALTY] This protein is a component of the oligopeptide permease, a binding protein-dependent transport system, it binds peptides up to five amino acids long with high affinity.
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b3/1b32_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1b32 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
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.
-
===OLIGO-PEPTIDE BINDING PROTEIN (OPPA) COMPLEXED WITH KMK===
+
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<ref>PMID:10438628</ref>
-
{{ABSTRACT_PUBMED_10438628}}
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
==About this Structure==
+
<div class="pdbe-citations 1b32" style="background-color:#fffaf0;"></div>
-
[[1b32]] is a 2 chain structure of [[Oligopeptide-binding protein]] with sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_typhimurium Salmonella enterica subsp. enterica serovar typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B32 OCA].
+
==See Also==
==See Also==
-
*[[Oligopeptide-binding protein|Oligopeptide-binding protein]]
+
*[[ABC transporter 3D structures|ABC transporter 3D structures]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
<ref group="xtra">PMID:010438628</ref><references group="xtra"/>
+
__TOC__
-
[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]
+
</StructureSection>
-
[[Category: Tame, J R.H.]]
+
[[Category: Large Structures]]
-
[[Category: Wilkinson, A J.]]
+
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
-
[[Category: Peptide binding protein]]
+
[[Category: Tame JRH]]
-
[[Category: Peptide transport]]
+
[[Category: Wilkinson AJ]]

Current revision

OLIGO-PEPTIDE BINDING PROTEIN (OPPA) COMPLEXED WITH KMK

PDB ID 1b32

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1b32"
Personal tools