1hxd

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[[Image:1hxd.gif|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF E. COLI BIOTIN REPRESSOR WITH BOUND BIOTIN==
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|PDB= 1hxd |SIZE=350|CAPTION= <scene name='initialview01'>1hxd</scene>, resolution 2.4&Aring;
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<StructureSection load='1hxd' size='340' side='right'caption='[[1hxd]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=BTN:BIOTIN'>BTN</scene>
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<table><tr><td colspan='2'>[[1hxd]] 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=1HXD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HXD FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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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]] 2.4&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTN:BIOTIN'>BTN</scene></td></tr>
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|DOMAIN=
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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=1hxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hxd OCA], [https://pdbe.org/1hxd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hxd RCSB], [https://www.ebi.ac.uk/pdbsum/1hxd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hxd ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1bia|1BIA]], [[1bib|1BIB]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hxd OCA], [http://www.ebi.ac.uk/pdbsum/1hxd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hxd RCSB]</span>
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== Function ==
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}}
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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/hx/1hxd_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=1hxd ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The Escherichia coli biotin repressor binds to the biotin operator to repress transcription of the biotin biosynthetic operon. In this work, a structure determined by x-ray crystallography of a complex of the repressor bound to biotin, which also functions as an activator of DNA binding by the biotin repressor (BirA), is described. In contrast to the monomeric aporepressor, the complex is dimeric with an interface composed in part of an extended beta-sheet. Model building, coupled with biochemical data, suggests that this is the dimeric form of BirA that binds DNA. Segments of three surface loops that are disordered in the aporepressor structure are located in the interface region of the dimer and exhibit greater order than was observed in the aporepressor structure. The results suggest that the corepressor of BirA causes a disorder-to-order transition that is a prerequisite to repressor dimerization and DNA binding.
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'''CRYSTAL STRUCTURE OF E. COLI BIOTIN REPRESSOR WITH BOUND BIOTIN'''
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Corepressor-induced organization and assembly of the biotin repressor: a model for allosteric activation of a transcriptional regulator.,Weaver LH, Kwon K, Beckett D, Matthews BW Proc Natl Acad Sci U S A. 2001 May 22;98(11):6045-50. Epub 2001 May 15. PMID:11353844<ref>PMID:11353844</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1hxd" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The Escherichia coli biotin repressor binds to the biotin operator to repress transcription of the biotin biosynthetic operon. In this work, a structure determined by x-ray crystallography of a complex of the repressor bound to biotin, which also functions as an activator of DNA binding by the biotin repressor (BirA), is described. In contrast to the monomeric aporepressor, the complex is dimeric with an interface composed in part of an extended beta-sheet. Model building, coupled with biochemical data, suggests that this is the dimeric form of BirA that binds DNA. Segments of three surface loops that are disordered in the aporepressor structure are located in the interface region of the dimer and exhibit greater order than was observed in the aporepressor structure. The results suggest that the corepressor of BirA causes a disorder-to-order transition that is a prerequisite to repressor dimerization and DNA binding.
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*[[Biotin Protein Ligase 3D structures|Biotin Protein Ligase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1HXD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HXD OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Corepressor-induced organization and assembly of the biotin repressor: a model for allosteric activation of a transcriptional regulator., Weaver LH, Kwon K, Beckett D, Matthews BW, Proc Natl Acad Sci U S A. 2001 May 22;98(11):6045-50. Epub 2001 May 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11353844 11353844]
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[[Category: Biotin--[acetyl-CoA-carboxylase] ligase]]
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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: Beckett, D.]]
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[[Category: Beckett D]]
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[[Category: Kwon, K.]]
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[[Category: Kwon K]]
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[[Category: Ruparelia, S.]]
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[[Category: Ruparelia S]]
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[[Category: Streaker, E D.]]
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[[Category: Streaker ED]]
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[[Category: biotin]]
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[[Category: dna-binding]]
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[[Category: ligase]]
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[[Category: repressor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:11:40 2008''
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Current revision

CRYSTAL STRUCTURE OF E. COLI BIOTIN REPRESSOR WITH BOUND BIOTIN

PDB ID 1hxd

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