2abd

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(Difference between revisions)

Revision as of 08:19, 11 September 2015

THE THREE-DIMENSIONAL STRUCTURE OF ACYL-COENZYME A BINDING PROTEIN FROM BOVINE LIVER. STRUCTURAL REFINEMENT USING HETERONUCLEAR MULTIDIMENSIONAL NMR SPECTROSCOPY

Structural highlights

2abd is a 1 chain structure with sequence from Bovin. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[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.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The 3D structure of bovine recombinant acyl-coenzyme A binding protein has been determined using multidimensional heteronuclear magnetic resonance spectroscopy in a study that combines investigations of 15N-labeled and unlabeled protein. The present structure determination is a refinement of the structure previously determined (Andersen, K.V. and Poulsen, F.M. (1992) J. Mol. Biol., 226, 1131-1141). It is based on 1096 distance restraints and 124 dihedral angle restraints of which 69 are for phi-angles and 8 for chiral centers and 47 for prochiral centers. The new experimental input for the structure determination has provided an increase of 263 distance restraints, 5 phi-angle restraints, and 32 chi-angle restraints in 2 chiral centers, and 31 prochiral centers restraining an additional 23 chi 1, 8 chi 2, and 1 chi 3 angles. The increase of 300 distance and dihedral angle restraints representing an additional 30% of input parameters for the structure determination has been shown to be in agreement with the first structure. A set of 29 structures has been calculated and each of the structures has been compared to a mean structure to give an atomic root mean square deviation of 0.44 +/- 0.12 A (1 A is 0.1 nm) for the backbone atoms C, C alpha, and N in the four alpha-helices A1, residues 4-15, A2, residues 21-36, A3, residues 51-62 and A4, residues 65-84. The loop-region of residues Gly45-Lys50 could not be defined by the restraints obtained by NMR. The program PRONTO has been used for the spectrum analysis, assignment of the individual nuclear Overhauser effects, the integration of the cross peaks, and the measurement of the coupling constants. The programs DIANA, X-PLOR and INSIGHT have been used in the structure calculations and evaluations.

The three-dimensional structure of acyl-coenzyme A binding protein from bovine liver: structural refinement using heteronuclear multidimensional NMR spectroscopy.,Andersen KV, Poulsen FM J Biomol NMR. 1993 May;3(3):271-84. PMID:8358232^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ van Aalten DM, Milne KG, Zou JY, Kleywegt GJ, Bergfors T, Ferguson MA, Knudsen J, Jones TA. Binding site differences revealed by crystal structures of Plasmodium falciparum and bovine acyl-CoA binding protein. J Mol Biol. 2001 May 25;309(1):181-92. PMID:11491287 doi:10.1006/jmbi.2001.4749
↑ Andersen KV, Poulsen FM. The three-dimensional structure of acyl-coenzyme A binding protein from bovine liver: structural refinement using heteronuclear multidimensional NMR spectroscopy. J Biomol NMR. 1993 May;3(3):271-84. PMID:8358232

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2abd"

Categories: Bovin | Andersen, K V | Poulsen, F M | Acyl-coenzyme a binding protein

@@ Line 2: / Line 2: @@
 <StructureSection load='2abd' size='340' side='right' caption='[[2abd]], [[NMR_Ensembles_of_Models | 29 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2abd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ABD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ABD FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2abd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ABD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ABD FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2abd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2abd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2abd RCSB], [http://www.ebi.ac.uk/pdbsum/2abd PDBsum]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2abd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2abd OCA], [http://pdbe.org/2abd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2abd RCSB], [http://www.ebi.ac.uk/pdbsum/2abd PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 25: / Line 25: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2abd" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Bos taurus]]
+[[Category: Bovin]]
 [[Category: Andersen, K V]]
 [[Category: Poulsen, F M]]
 [[Category: Acyl-coenzyme a binding protein]]

2abd

From Proteopedia

Revision as of 08:19, 11 September 2015

THE THREE-DIMENSIONAL STRUCTURE OF ACYL-COENZYME A BINDING PROTEIN FROM BOVINE LIVER. STRUCTURAL REFINEMENT USING HETERONUCLEAR MULTIDIMENSIONAL NMR SPECTROSCOPY

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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