1hb8: Difference between revisions

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-[[Image:1hb8.png|left|200px]]
-{{STRUCTURE_1hb8|  PDB=1hb8  |  SCENE=  }}
+==Structure of bovine Acyl-CoA binding protein in tetragonal crystal form==
+<StructureSection load='1hb8' size='340' side='right'caption='[[1hb8]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1hb8]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HB8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HB8 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]] 2&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1hb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hb8 OCA], [https://pdbe.org/1hb8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hb8 RCSB], [https://www.ebi.ac.uk/pdbsum/1hb8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hb8 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ACBP_BOVIN ACBP_BOVIN] Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor.<ref>PMID:11491287</ref>
+== 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/hb/1hb8_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1hb8 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Acyl-CoA binding protein (ACBP) maintains a pool of fatty acyl-CoA molecules in the cell and plays a role in fatty acid metabolism. The biochemical properties of Plasmodium falciparum ACBP are described together with the 2.0 A resolution crystal structures of a P. falciparum ACBP-acyl-CoA complex and of bovine ACBP in two crystal forms. Overall, the bovine ACBP crystal structures are similar to the NMR structures published previously; however, the bovine and parasite ACBP structures are less similar. The parasite ACBP is shown to have a different ligand-binding pocket, leading to an acyl-CoA binding specificity different from that of bovine ACBP. Several non-conservative differences in residues that interact with the ligand were identified between the mammalian and parasite ACBPs. These, together with measured binding-specificity differences, suggest that there is a potential for the design of molecules that might selectively block the acyl-CoA binding site.
-===STRUCTURE OF BOVINE ACYL-COA BINDING PROTEIN IN TETRAGONAL CRYSTAL FORM===
+Binding site differences revealed by crystal structures of Plasmodium falciparum and bovine acyl-CoA binding protein.,van Aalten DM, Milne KG, Zou JY, Kleywegt GJ, Bergfors T, Ferguson MA, Knudsen J, Jones TA J Mol Biol. 2001 May 25;309(1):181-92. PMID:11491287<ref>PMID:11491287</ref>
-{{ABSTRACT_PUBMED_11491287}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 1hb8" style="background-color:#fffaf0;"></div>
-[[1hb8]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HB8 OCA].
+== References ==
+<references/>
-==Reference==
+__TOC__
-<ref group="xtra">PMID:011491287</ref><references group="xtra"/>
+</StructureSection>
-[[Category: Bergfors, T.]]
+[[Category: Bos taurus]]
-[[Category: Jones, T A.]]
+[[Category: Large Structures]]
-[[Category: Kleywegt, G J.]]
+[[Category: Bergfors T]]
-[[Category: Knudsen, J.]]
+[[Category: Jones TA]]
-[[Category: Zou, J Y.]]
+[[Category: Kleywegt GJ]]
-[[Category: Acyl-coa]]
+[[Category: Knudsen J]]
-[[Category: Acyl-coenzyme a binding protein]]
+[[Category: Zou JY]]
-[[Category: Binding protein]]