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| | <StructureSection load='1sax' size='340' side='right'caption='[[1sax]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='1sax' size='340' side='right'caption='[[1sax]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1sax]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Staan Staan]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SAX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1SAX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1sax]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_N315 Staphylococcus aureus subsp. aureus N315]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SAX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SAX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1okr|1okr]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mecI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=158879 STAAN])</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=1sax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sax OCA], [https://pdbe.org/1sax PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sax RCSB], [https://www.ebi.ac.uk/pdbsum/1sax PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sax ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1sax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sax OCA], [http://pdbe.org/1sax PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sax RCSB], [http://www.ebi.ac.uk/pdbsum/1sax PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1sax ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MECI_STAAU MECI_STAAU]] Transcriptional repressor that constitutively blocks the transcription of the gene for the penicillin-binding protein MecA. Binds DNA as a dimer (By similarity). | + | [https://www.uniprot.org/uniprot/MECI_STAAN MECI_STAAN] Transcriptional repressor that constitutively blocks the transcription of the gene for the penicillin-binding protein MecA. Binds palindromic DNA with the sequence 5'-TACA-[AT]-N-TGTA-3'. Regulates genes involved in antibiotic resistance. Binds DNA as a dimer. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Staan]] | + | [[Category: Staphylococcus aureus subsp. aureus N315]] |
| - | [[Category: Coll, M]] | + | [[Category: Coll M]] |
| - | [[Category: Garcia-Castellanos, R]] | + | [[Category: Garcia-Castellanos R]] |
| - | [[Category: Gomis-Ruth, F X]] | + | [[Category: Gomis-Ruth FX]] |
| - | [[Category: Mallorqui-Fernandez, G]] | + | [[Category: Mallorqui-Fernandez G]] |
| - | [[Category: Marrero, A]] | + | [[Category: Marrero A]] |
| - | [[Category: Potempa, J]] | + | [[Category: Potempa J]] |
| - | [[Category: Transcription-dna complex]]
| + | |
| - | [[Category: Winged helix-turn-helix]]
| + | |
| Structural highlights
Function
MECI_STAAN Transcriptional repressor that constitutively blocks the transcription of the gene for the penicillin-binding protein MecA. Binds palindromic DNA with the sequence 5'-TACA-[AT]-N-TGTA-3'. 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
Bacterial resistance to antibiotics poses a serious worldwide public health problem due to the high morbidity and mortality caused by infectious diseases. Most hospital-onset infections are associated with methicillin-resistant Staphylococcus aureus (MRSA) strains that have acquired multiple drug resistance to beta-lactam antibiotics. In a response to antimicrobial stress, nearly all clinical MRSA isolates produce beta-lactamase (BlaZ) and a penicillin-binding protein with low affinity for beta-lactam antibiotics (PBP2a, also known as PBP2' or MecA). Both effectors are regulated by homologous signal transduction systems consisting of a sensor/transducer and a transcriptional repressor. MecI (methicillin repressor) blocks mecA but also blaZ transcription and that of itself and the co-transcribed sensor/transducer. The structure of MecI in complex with a cognate operator double-stranded DNA reveals a homodimeric arrangement with a novel C-terminal spiral staircase dimerization domain responsible for dimer integrity. Each protomer interacts with the DNA major groove through a winged helix DNA-binding domain and specifically recognizes the nucleotide sequence 5'-Gua-Thy-Ade-X-Thy-3'. This results in an unusual convex bending of the DNA helix. The structure of this first molecular determinant of methicillin resistance in complex with its target DNA provides insights into its regulatory mechanism and paves the way for new antimicrobial strategies against MRSA.
On the transcriptional regulation of methicillin resistance: MecI repressor in complex with its operator.,Garcia-Castellanos R, Mallorqui-Fernandez G, Marrero A, Potempa J, Coll M, Gomis-Ruth FX J Biol Chem. 2004 Apr 23;279(17):17888-96. Epub 2004 Feb 11. PMID:14960592[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Garcia-Castellanos R, Mallorqui-Fernandez G, Marrero A, Potempa J, Coll M, Gomis-Ruth FX. On the transcriptional regulation of methicillin resistance: MecI repressor in complex with its operator. J Biol Chem. 2004 Apr 23;279(17):17888-96. Epub 2004 Feb 11. PMID:14960592 doi:10.1074/jbc.M313123200
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