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1bia

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(New page: 200px<br /><applet load="1bia" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bia, resolution 2.3&Aring;" /> '''THE E. COLI BIOTIN HO...)
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[[Image:1bia.gif|left|200px]]<br /><applet load="1bia" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1bia, resolution 2.3&Aring;" />
 
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'''THE E. COLI BIOTIN HOLOENZYME SYNTHETASE(SLASH)BIO REPRESSOR CRYSTAL STRUCTURE DELINEATES THE BIOTIN AND DNA-BINDING DOMAINS'''<br />
 
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==Overview==
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==THE E. COLI BIOTIN HOLOENZYME SYNTHETASE(SLASH)BIO REPRESSOR CRYSTAL STRUCTURE DELINEATES THE BIOTIN AND DNA-BINDING DOMAINS==
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The three-dimensional structure of BirA, the repressor of the Escherichia, coli biotin biosynthetic operon, has been determined by x-ray, crystallography and refined to a crystallographic residual of 19.0% at, 2.3-A resolution. BirA is a sequence-specific DNA-binding protein that, also catalyzes the formation of biotinyl-5'-adenylate from biotin and ATP, and transfers the biotin moiety to other proteins. The level of biotin, biosynthetic enzymes in the cell is controlled by the amount of, biotinyl-5'-adenylate, which is the BirA corepressor. The structure, provides an example of a transcription factor that is also an enzyme. The, structure of BirA is highly asymmetric and consists of three domains. The, N-terminal domain is mostly alpha-helical, contains a helix-turn-helix, DNA-binding motif, and is loosely connected to the remainder of the, molecule. The central domain consists of a seven-stranded mixed beta-sheet, with alpha-helices covering one face. The other side of the sheet is, largely solvent-exposed and contains the active site. The C-terminal, domain comprises a six-stranded, antiparallel beta-sheet sandwich. The, location of biotin binding is consistent with mutations that affect, enzymatic activity. A nearby loop has a sequence that has been associated, with phosphate binding in other proteins. It is inferred that ATP binds in, this region, adjacent to the biotin. It is proposed that the binding of, corepressor to monomeric BirA may promote DNA binding by facilitating the, formation of a multimeric BirA-corepressor-DNA complex. The structural, details of this complex remain an open question, however.
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<StructureSection load='1bia' size='340' side='right'caption='[[1bia]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1bia]] is a 1 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=1BIA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BIA 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]] 2.3&#8491;</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=1bia FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bia OCA], [https://pdbe.org/1bia PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bia RCSB], [https://www.ebi.ac.uk/pdbsum/1bia PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bia ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/BIRA_ECOLI BIRA_ECOLI] Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon.<ref>PMID:6129246</ref> <ref>PMID:2667763</ref> <ref>PMID:8003500</ref> <ref>PMID:12527300</ref>
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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/bi/1bia_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=1bia 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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1BIA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Biotin--[acetyl-CoA-carboxylase]_ligase Biotin--[acetyl-CoA-carboxylase] ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.15 6.3.4.15] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BIA OCA].
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*[[Biotin Protein Ligase 3D structures|Biotin Protein Ligase 3D structures]]
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== References ==
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==Reference==
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<references/>
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Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains., Wilson KP, Shewchuk LM, Brennan RG, Otsuka AJ, Matthews BW, Proc Natl Acad Sci U S A. 1992 Oct 1;89(19):9257-61. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1409631 1409631]
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__TOC__
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[[Category: Biotin--[acetyl-CoA-carboxylase] ligase]]
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</StructureSection>
[[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: Matthews, B.W.]]
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[[Category: Matthews BW]]
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[[Category: Shewchuk, L.M.]]
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[[Category: Shewchuk LM]]
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[[Category: Wilson, K.P.]]
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[[Category: Wilson KP]]
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[[Category: transcription regulation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:40:35 2007''
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Current revision

THE E. COLI BIOTIN HOLOENZYME SYNTHETASE(SLASH)BIO REPRESSOR CRYSTAL STRUCTURE DELINEATES THE BIOTIN AND DNA-BINDING DOMAINS

PDB ID 1bia

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