1k1c

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{{Seed}}
 
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[[Image:1k1c.png|left|200px]]
 
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==Solution Structure of Crh, the Bacillus subtilis Catabolite Repression HPr==
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The line below this paragraph, containing "STRUCTURE_1k1c", creates the "Structure Box" on the page.
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<StructureSection load='1k1c' size='340' side='right'caption='[[1k1c]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1k1c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K1C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K1C FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1k1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k1c OCA], [https://pdbe.org/1k1c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k1c RCSB], [https://www.ebi.ac.uk/pdbsum/1k1c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k1c ProSAT]</span></td></tr>
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{{STRUCTURE_1k1c| PDB=1k1c | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CRH_BACSU CRH_BACSU] Along with seryl-phosphorylated HPr, phosphorylated Crh is implicated in carbon catabolite repression (CCR) of levanase, inositol dehydrogenase, and beta-xylosidase. Exerts its effect on CCR by interacting with CcpA.<ref>PMID:9237995</ref> <ref>PMID:16316990</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k1/1k1c_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1k1c ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The solution structure and dynamics of the Bacillus subtilis HPr-like protein, Crh, have been investigated using NMR spectroscopy. Crh exhibits high sequence identity (45 %) to the histidine-containing protein (HPr), a phospho-carrier protein of the phosphoenolpyruvate (PEP):carbohydrate phosphotransferase system, but contains no catalytic His15, the site of PEP-dependent phosphorylation in HPr. Crh also forms a mixture of monomers and dimers in solution whereas HPr is known to be monomeric. Complete backbone and side-chain assignments were obtained for the monomeric form, and 60 % of the dimer backbone resonances; allowing the identification of the Crh dimer interface from chemical-shift mapping. The conformation of Crh was determined to a precision of 0.46(+/-0.06) A for the backbone atoms, and 1.01(+/-0.08) A for the heavy atoms. The monomer structure is similar to that of known HPr 2.67(+/-0.22) A (C(alpha) rmsd), but has a few notable differences, including a change in the orientation of one of the helices (B), and a two-residue shift in beta-sheet pairing of the N-terminal strand with the beta4 strand. This shift results in a shortening of the surface loop present in HPr and consequently provides a flatter surface in the region of dimerisation contact, which may be related to the different oligomeric nature of these two proteins. A binding site of phospho-serine(P-Ser)-Crh with catabolite control protein A (CcpA) is proposed on the basis of highly conserved surface side-chains between Crh and HPr. This binding site is consistent with the model of a dimer-dimer interaction between P-Ser-Crh and CcpA. (15)N relaxation measured in the monomeric form also identified differential local mobility in the helix B which is located in the vicinity of this site.
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===Solution Structure of Crh, the Bacillus subtilis Catabolite Repression HPr===
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Solution structure and dynamics of Crh, the Bacillus subtilis catabolite repression HPr.,Favier A, Brutscher B, Blackledge M, Galinier A, Deutscher J, Penin F, Marion D J Mol Biol. 2002 Mar 15;317(1):131-44. PMID:11916384<ref>PMID:11916384</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_11916384}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1k1c" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 11916384 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11916384}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1K1C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K1C OCA].
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==Reference==
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Solution structure and dynamics of Crh, the Bacillus subtilis catabolite repression HPr., Favier A, Brutscher B, Blackledge M, Galinier A, Deutscher J, Penin F, Marion D, J Mol Biol. 2002 Mar 15;317(1):131-44. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11916384 11916384]
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[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Blackledge, M.]]
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[[Category: Blackledge M]]
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[[Category: Brutscher, B.]]
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[[Category: Brutscher B]]
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[[Category: Deutscher, J.]]
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[[Category: Deutscher J]]
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[[Category: Favier, A.]]
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[[Category: Favier A]]
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[[Category: Galinier, A.]]
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[[Category: Galinier A]]
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[[Category: Marion, D.]]
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[[Category: Marion D]]
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[[Category: Penin, F.]]
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[[Category: Penin F]]
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[[Category: Carbon catabolite repression]]
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[[Category: Open-faced b-sandwich]]
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[[Category: Phosphotransferase system]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 21:16:21 2008''
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Current revision

Solution Structure of Crh, the Bacillus subtilis Catabolite Repression HPr

PDB ID 1k1c

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