1dv1

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(New page: 200px<br /><applet load="1dv1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dv1, resolution 1.90&Aring;" /> '''STRUCTURE OF BIOTIN ...)
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[[Image:1dv1.jpg|left|200px]]<br /><applet load="1dv1" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1dv1, resolution 1.90&Aring;" />
 
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'''STRUCTURE OF BIOTIN CARBOXYLASE (APO)'''<br />
 
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==Overview==
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==STRUCTURE OF BIOTIN CARBOXYLASE (APO)==
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Acetyl-CoA carboxylase catalyzes the first committed step in fatty acid, synthesis. In Escherichia coli, the enzyme is composed of three distinct, protein components: biotin carboxylase, biotin carboxyl carrier protein, and carboxyltransferase. The biotin carboxylase component has served for, many years as a paradigm for mechanistic studies devoted toward, understanding more complicated biotin-dependent carboxylases. The, three-dimensional x-ray structure of an unliganded form of E. coli biotin, carboxylase was originally solved in 1994 to 2.4-A resolution. This study, revealed the architecture of the enzyme and demonstrated that the protein, belongs to the ATP-grasp superfamily. Here we describe the, three-dimensional structure of the E. coli biotin carboxylase complexed, with ATP and determined to 2.5-A resolution. The major conformational, change that occurs upon nucleotide binding is a rotation of approximately, 45(o) of one domain relative to the other domains thereby closing off the, active site pocket. Key residues involved in binding the nucleotide to the, protein include Lys-116, His-236, and Glu-201. The backbone amide groups, of Gly-165 and Gly-166 participate in hydrogen bonding interactions with, the phosphoryl oxygens of the nucleotide. A comparison of this closed form, of biotin carboxylase with carbamoyl-phosphate synthetase is presented.
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<StructureSection load='1dv1' size='340' side='right'caption='[[1dv1]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1dv1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DV1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DV1 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dv1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dv1 OCA], [https://pdbe.org/1dv1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dv1 RCSB], [https://www.ebi.ac.uk/pdbsum/1dv1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dv1 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ACCC_ECOLI ACCC_ECOLI] This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dv/1dv1_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1dv1 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1DV1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Biotin_carboxylase Biotin carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.14 6.3.4.14] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DV1 OCA].
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*[[Acetyl-CoA carboxylase 3D structures|Acetyl-CoA carboxylase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Movement of the biotin carboxylase B-domain as a result of ATP binding., Thoden JB, Blanchard CZ, Holden HM, Waldrop GL, J Biol Chem. 2000 May 26;275(21):16183-90. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10821865 10821865]
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[[Category: Biotin carboxylase]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Blanchard, C.Z]]
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[[Category: Blanchard CZ]]
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[[Category: Holden, H.M.]]
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[[Category: Holden HM]]
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[[Category: Thoden, J.B.]]
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[[Category: Thoden JB]]
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[[Category: Waldrop, G.W]]
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[[Category: Waldrop GL]]
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[[Category: PO4]]
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[[Category: atp-grasp]]
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[[Category: biotin-dependent]]
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[[Category: carboxylase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:36:24 2007''
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Current revision

STRUCTURE OF BIOTIN CARBOXYLASE (APO)

PDB ID 1dv1

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