1p6r

From Proteopedia

(Difference between revisions)

Current revision

Solution structure of the DNA binding domain of the repressor BlaI.

Structural highlights

1p6r is a 1 chain structure with sequence from Bacillus licheniformis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BLAI_BACLI Transcriptional repressor that constitutively blocks expression of beta-lactamase. Regulates genes involved in antibiotic resistance. Binds DNA as a dimer.

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

beta-Lactamase and penicillin-binding protein PBP2' mediate staphylococcal resistance to beta-lactam antibiotics, which are otherwise highly clinically effective. Two repressors (BlaI and MecI) regulate expression of these inducible proteins. Here, we present the first solution structure of the 82 amino acid residue DNA-binding domain of Bacillus licheniformis BlaI which is very similar in primary sequence to the medically significant Staphyloccocal BlaI and MecI proteins. This structure is composed of a compact core of three alpha-helices and a three-stranded beta-sheet typical of the winged helix protein (WHP) family. The protein/DNA complex was studied by NMR chemical shift comparison between the free and complexed forms of BlaI. Residues involved in DNA interaction were identified and a WHP canonical model of interaction with the operators is proposed. In this model, specific contacts occur between the base-pairs of the TACA motif and conserved amino acid residues of the repressor helix H3. These results help toward understanding the repression and induction mechanism of the genes coding for beta-lactamase and PBP2'.

Solution structural study of BlaI: implications for the repression of genes involved in beta-lactam antibiotic resistance.,Melckebeke HV, Vreuls C, Gans P, Filee P, Llabres G, Joris B, Simorre JP J Mol Biol. 2003 Oct 31;333(4):711-20. PMID:14568532^[1]

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

References

↑ Melckebeke HV, Vreuls C, Gans P, Filee P, Llabres G, Joris B, Simorre JP. Solution structural study of BlaI: implications for the repression of genes involved in beta-lactam antibiotic resistance. J Mol Biol. 2003 Oct 31;333(4):711-20. PMID:14568532

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/1p6r"

@@ Line 1: / Line 1: @@
 ==Solution structure of the DNA binding domain of the repressor BlaI.==
-<StructureSection load='1p6r' size='340' side='right'caption='[[1p6r]], [[NMR_Ensembles_of_Models | 19 NMR models]]' scene=''>
+<StructureSection load='1p6r' size='340' side='right'caption='[[1p6r]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1p6r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"denitrobacillus_licheniformis"_(weigmann_1898)_verhoeven_1952 "denitrobacillus licheniformis" (weigmann 1898) verhoeven 1952]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P6R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P6R FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1p6r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P6R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P6R FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BLAI OR PENI ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1402 "Denitrobacillus licheniformis" (Weigmann 1898) Verhoeven 1952])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1p6r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p6r OCA], [https://pdbe.org/1p6r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p6r RCSB], [https://www.ebi.ac.uk/pdbsum/1p6r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p6r ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/BLAI_BACLI BLAI_BACLI]] Transcriptional repressor that constitutively blocks expression of beta-lactamase. Regulates genes involved in antibiotic resistance. Binds DNA as a dimer.
+[https://www.uniprot.org/uniprot/BLAI_BACLI BLAI_BACLI] Transcriptional repressor that constitutively blocks expression of beta-lactamase. Regulates genes involved in antibiotic resistance. Binds DNA as a dimer.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 32: @@
 __TOC__
 </StructureSection>
+[[Category: Bacillus licheniformis]]
 [[Category: Large Structures]]
-[[Category: Filee, P]]
+[[Category: Filee P]]
-[[Category: Gans, P]]
+[[Category: Gans P]]
-[[Category: Joris, B]]
+[[Category: Joris B]]
-[[Category: Llabres, G]]
+[[Category: Llabres G]]
-[[Category: Melckebeke, H V]]
+[[Category: Melckebeke HV]]
-[[Category: Simorre, J P]]
+[[Category: Simorre JP]]
-[[Category: Vreuls, C]]
+[[Category: Vreuls C]]
-[[Category: Bacterial resistance to antibiotic]]
-[[Category: Dna-binding]]
-[[Category: Repressor]]
-[[Category: Transcription]]
-[[Category: Transcription regulation]]
-[[Category: Winged helix protein]]

1p6r

From Proteopedia

Current revision

Solution structure of the DNA binding domain of the repressor BlaI.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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