1hxd

From Proteopedia

(Difference between revisions)

Revision as of 10:42, 27 September 2017

CRYSTAL STRUCTURE OF E. COLI BIOTIN REPRESSOR WITH BOUND BIOTIN

Structural highlights

1hxd is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1bia, 1bib
Activity:	[acetyl-CoA-carboxylase_ligase Biotin--[acetyl-CoA-carboxylase] ligase], with EC number 6.3.4.15
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2] ^[3] ^[4]

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 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.

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^[5]

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

References

↑ Eisenberg MA, Prakash O, Hsiung SC. Purification and properties of the biotin repressor. A bifunctional protein. J Biol Chem. 1982 Dec 25;257(24):15167-73. PMID:6129246
↑ Cronan JE Jr. The E. coli bio operon: transcriptional repression by an essential protein modification enzyme. Cell. 1989 Aug 11;58(3):427-9. PMID:2667763
↑ Xu Y, Beckett D. Kinetics of biotinyl-5'-adenylate synthesis catalyzed by the Escherichia coli repressor of biotin biosynthesis and the stability of the enzyme-product complex. Biochemistry. 1994 Jun 14;33(23):7354-60. PMID:8003500
↑ Streaker ED, Beckett D. Coupling of protein assembly and DNA binding: biotin repressor dimerization precedes biotin operator binding. J Mol Biol. 2003 Jan 31;325(5):937-48. PMID:12527300 doi:http://dx.doi.org/10.1016/S0022283602013086
↑ Weaver LH, Kwon K, Beckett D, Matthews BW. Corepressor-induced organization and assembly of the biotin repressor: a model for allosteric activation of a transcriptional regulator. Proc Natl Acad Sci U S A. 2001 May 22;98(11):6045-50. Epub 2001 May 15. PMID:11353844 doi:10.1073/pnas.111128198

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1hxd"

@@ Line 1: / Line 1: @@
 ==CRYSTAL STRUCTURE OF E. COLI BIOTIN REPRESSOR WITH BOUND BIOTIN==
 <StructureSection load='1hxd' size='340' side='right' caption='[[1hxd]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1hxd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HXD FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1hxd]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HXD FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BTN:BIOTIN'>BTN</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bia|1bia]], [[1bib|1bib]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></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=1hxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hxd OCA], [http://pdbe.org/1hxd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hxd RCSB], [http://www.ebi.ac.uk/pdbsum/1hxd PDBsum]</span></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=1hxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hxd OCA], [http://pdbe.org/1hxd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hxd RCSB], [http://www.ebi.ac.uk/pdbsum/1hxd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hxd ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
     <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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 1hxd" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Biotin Protein Ligase|Biotin Protein Ligase]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
 [[Category: Beckett, D]]
 [[Category: Kwon, K]]

1hxd

From Proteopedia

Revision as of 10:42, 27 September 2017

CRYSTAL STRUCTURE OF E. COLI BIOTIN REPRESSOR WITH BOUND BIOTIN

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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