5y9q

<StructureSection load='5y9q' size='340' side='right' caption='[[5y9q]], [[Resolution|resolution]] 1.95&Aring;' scene=''>

<table><tr><td colspan='2'>[[5y9q]] is a 2 chain structure with sequence from [http://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=5Y9Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y9Q FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">oxyR, BMF23_07630, ERS073071_00913, ERS073583_00871 ([http://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='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=5y9q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y9q OCA], [http://pdbe.org/5y9q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y9q RCSB], [http://www.ebi.ac.uk/pdbsum/5y9q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y9q ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Catabolite control protein E (CcpE) is a LysR-type transcriptional regulator that positively regulates the transcription of the first two enzymes of the TCA cycle, namely, citZ and citB, by sensing accumulated intracellular citrate. CcpE comprises an N-terminal DNA-binding domain and a C-terminal regulatory domain (RD) and senses citrate with conserved arginine residues in the RD. Although the crystal structure of the apo SaCcpE-RD has been reported, the citrate-responsive and DNA-binding mechanisms by which CcpE regulates TCA activity remain unclear. Here, we report the crystal structure of the apo and citrate-bound SaCcpE-RDs. The SaCcpE-RD exhibits conformational changes between the two subdomains via hinge motion of the central beta4 and beta10 strands. The citrate molecule is located in a positively charged cavity between the two subdomains and interacts with the highly conserved Ser98, Leu100, Arg145, and Arg256 residues. Compared with that of the apo SaCcpE-RD, the distance between the two subdomains of the citrate-bound SaCcpE-RD is more than approximately 3 A due to the binding of the citrate molecule, and this form exhibits a closed structure. The SaCcpE-RD exhibits various citrate-binding-independent conformational changes at the contacting interface. The SaCcpE-RD prefers the dimeric state in solution, whereas the SaCcpE-FL prefers the tetrameric state. Our results provide insight into the molecular function of SaCcpE.

Structural and Biochemical Analysis of the Citrate-Responsive Mechanism of the Regulatory Domain of Catabolite Control Protein E from Staphylococcus aureus.,Chen J, Shang F, Wang L, Zou L, Bu T, Jin L, Dong Y, Ha NC, Quan C, Nam KH, Xu Y Biochemistry. 2018 Oct 3. doi: 10.1021/acs.biochem.8b00671. PMID:30252448<ref>PMID:30252448</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 5y9q" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Chen, J]]

[[Category: Shang, F]]

[[Category: Wang, L]]

[[Category: Xu, Y]]

[[Category: Dimer]]

[[Category: Regulatory domain]]

[[Category: Transcription]]