1u2w: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
Line 3: Line 3:
<StructureSection load='1u2w' size='340' side='right'caption='[[1u2w]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='1u2w' size='340' side='right'caption='[[1u2w]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1u2w]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U2W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U2W FirstGlance]. <br>
<table><tr><td colspan='2'>[[1u2w]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U2W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U2W FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.9&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cadC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1u2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u2w OCA], [https://pdbe.org/1u2w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u2w RCSB], [https://www.ebi.ac.uk/pdbsum/1u2w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u2w ProSAT]</span></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=1u2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u2w OCA], [https://pdbe.org/1u2w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u2w RCSB], [https://www.ebi.ac.uk/pdbsum/1u2w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u2w ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/CADC_STAAU CADC_STAAU]] Metal-binding repressor for the cad operon. Involved in resistance to heavy metals, such as cadmium, bismuth, zinc or lead. Binds 2 metal ions per subunit. Metal binding to the N-terminal regulatory site causes the repressor to dissociate from the DNA.<ref>PMID:7543476</ref> <ref>PMID:11278706</ref> <ref>PMID:12176999</ref> <ref>PMID:11941514</ref> <ref>PMID:19286656</ref>
[https://www.uniprot.org/uniprot/CADC_STAAU CADC_STAAU] Metal-binding repressor for the cad operon. Involved in resistance to heavy metals, such as cadmium, bismuth, zinc or lead. Binds 2 metal ions per subunit. Metal binding to the N-terminal regulatory site causes the repressor to dissociate from the DNA.<ref>PMID:7543476</ref> <ref>PMID:11278706</ref> <ref>PMID:12176999</ref> <ref>PMID:11941514</ref> <ref>PMID:19286656</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 20: Line 20:
</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=1u2w 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=1u2w ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Staphylococcus aureus plasmid pI258 cadCA operon encodes a P-type ATPase, CadA, that confers resistance to the heavy metals Cd(II), Zn(II), and Pb(II). Expression of this heavy-metal efflux pump is regulated by CadC, a homodimeric repressor that dissociates from the cad operator/promoter upon binding of Cd(II), Pb(II), or Zn(II). CadC is a member of the ArsR/SmtB family of metalloregulatory proteins. Here we report the X-ray crystal structure of CadC at 1.9 angstroms resolution. The dimensions of the protein dimer are approximately 30 angstroms by 40 angstroms by 70 angstroms. Each monomer contains six alpha-helices and a three-stranded beta-sheet. Helices 4 and 5 form a classic helix-turn-helix motif that is the putative DNA binding region. The alpha1 helix of one monomer crosses the dimer to approach the alpha4 helix of the other monomer, consistent with the previous proposal that these two regulatory metal binding sites for the inducer cadmium or lead are each formed by Cys-7 and Cys-11 from the N terminus of one monomer and Cys-58 and Cys-60 of the other monomer. Two nonregulatory metal binding sites containing zinc are formed between the two antiparallel alpha6 helices at the dimerization interface. This is the first reported three-dimensional structure of a member of the ArsR/SmtB family with regulatory metal binding sites at the DNA binding domain and the first structure of a transcription repressor that responds to the heavy metals Cd(II) and Pb(II).
Crystal structure of the Staphylococcus aureus pI258 CadC Cd(II)/Pb(II)/Zn(II)-responsive repressor.,Ye J, Kandegedara A, Martin P, Rosen BP J Bacteriol. 2005 Jun;187(12):4214-21. PMID:15937183<ref>PMID:15937183</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1u2w" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
Line 34: Line 25:
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Kandegedara, A]]
[[Category: Staphylococcus aureus]]
[[Category: Martin, P]]
[[Category: Kandegedara A]]
[[Category: Rosen, B P]]
[[Category: Martin P]]
[[Category: Ye, J]]
[[Category: Rosen BP]]
[[Category: Arsr/smtb family]]
[[Category: Ye J]]
[[Category: Cadmium]]
[[Category: Dna binding protein]]
[[Category: Lead]]
[[Category: Repressor]]
[[Category: Soft metal ion resistance]]

Revision as of 08:46, 1 May 2024

Crystal Structure of the Staphylococcus aureus pI258 CadC

1u2w, resolution 1.90Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1u2w&oldid=4141403"