1hbk: Difference between revisions

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[[Image:1hbk.gif|left|200px]]<br />
<applet load="1hbk" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1hbk, resolution 2.00&Aring;" />
'''ACYL-COA BINDING PROTEIN FROM PLASMODIUM FALCIPARUM'''<br />


==Overview==
==Acyl-CoA binding protein from Plasmodium falciparum==
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 ... [[http://ispc.weizmann.ac.il/pmbin/getpm?11491287 (full description)]]
<StructureSection load='1hbk' size='340' side='right'caption='[[1hbk]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1hbk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HBK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HBK 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=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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=1hbk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hbk OCA], [https://pdbe.org/1hbk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hbk RCSB], [https://www.ebi.ac.uk/pdbsum/1hbk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hbk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8IK57_PLAF7 Q8IK57_PLAF7]
== 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/1hbk_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=1hbk 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.


==About this Structure==
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>
1HBK is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]] with NI, COA and MYR as [[http://en.wikipedia.org/wiki/ligands ligands]]. Structure known Active Sites: COA, MYR, NI1 and NI2. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HBK OCA]].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11491287 11491287]
</div>
<div class="pdbe-citations 1hbk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Plasmodium falciparum]]
[[Category: Plasmodium falciparum]]
[[Category: Protein complex]]
[[Category: Van Aalten DMF]]
[[Category: Aalten, D.M.F.Van.]]
[[Category: COA]]
[[Category: MYR]]
[[Category: NI]]
[[Category: fatty acid metabolism]]
 
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