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1xvv

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(New page: 200px<br /><applet load="1xvv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xvv, resolution 2.40&Aring;" /> '''Crystal Structure of...)
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[[Image:1xvv.gif|left|200px]]<br /><applet load="1xvv" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1xvv, resolution 2.40&Aring;" />
 
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'''Crystal Structure of CaiB mutant D169A in complex with carnitinyl-CoA'''<br />
 
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==Overview==
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==Crystal Structure of CaiB mutant D169A in complex with carnitinyl-CoA==
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L-Carnitine (R-[-]-3-hydroxy-4-trimethylaminobutyrate) is found in both, eukaryotic and prokaryotic cells and participates in diverse processes, including long-chain fatty-acid transport and osmoprotection. The enzyme, crotonobetainyl/gamma-butyrobetainyl-CoA:carnitine CoA-transferase (CaiB;, E.C. 2.8.3.-) catalyzes the first step in carnitine metabolism, leading to, the final product gamma-butyrobetaine. The crystal structures of, Escherichia coli apo-CaiB, as well as its Asp169Ala mutant bound to CoA, and to carnitinyl-CoA, have been determined and refined to 1.6, 2.4, and, 2.4 A resolution, respectively. CaiB is composed of two identical circular, chains that together form an intertwined dimer. Each monomer consists of a, large domain, containing a Rossmann fold, and a small domain. The monomer, and dimer resemble those of formyl-CoA transferase from Oxalobacter, formigenes, as well as E. coli YfdW, a putative type-III CoA transferase, of unknown function. The CoA cofactor-binding site is formed at the, interface of the large domain of one monomer and the small domain from the, second monomer. Most of the protein-CoA interactions are formed with the, Rossmann fold domain. While the location of cofactor binding is similar in, the three proteins, the specific CoA-protein interactions vary somewhat, between CaiB, formyl-CoA transferase, and YfdW. CoA binding results in a, change in the relative positions of the large and small domains compared, with apo-CaiB. The observed carnitinyl-CoA product in crystals of the CaiB, Asp169Ala mutant cocrystallized with crotonoyl-CoA and carnitine could, result from (i) a catalytic mechanism involving a ternary enzyme-substrate, complex, independent of a covalent anhydride intermediate with Asp169, (ii) a spontaneous reaction of the substrates in solution, followed by, binding to the enzyme, or (iii) an involvement of another residue, substituting functionally for Asp169, such as Glu23.
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<StructureSection load='1xvv' size='340' side='right'caption='[[1xvv]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1xvv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XVV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XVV FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CCQ:L-CARNITINYL-COA+INNER+SALT'>CCQ</scene></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=1xvv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xvv OCA], [https://pdbe.org/1xvv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xvv RCSB], [https://www.ebi.ac.uk/pdbsum/1xvv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xvv ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CAIB_ECOLI CAIB_ECOLI] Catalyzes the reversible transfer of the CoA moiety from gamma-butyrobetainyl-CoA to L-carnitine to generate L-carnitinyl-CoA and gamma-butyrobetaine. Is also able to catalyze the reversible transfer of the CoA moiety from gamma-butyrobetainyl-CoA or L-carnitinyl-CoA to crotonobetaine to generate crotonobetainyl-CoA.<ref>PMID:11551212</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/xv/1xvv_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=1xvv 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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L-Carnitine (R-[-]-3-hydroxy-4-trimethylaminobutyrate) is found in both eukaryotic and prokaryotic cells and participates in diverse processes including long-chain fatty-acid transport and osmoprotection. The enzyme crotonobetainyl/gamma-butyrobetainyl-CoA:carnitine CoA-transferase (CaiB; E.C. 2.8.3.-) catalyzes the first step in carnitine metabolism, leading to the final product gamma-butyrobetaine. The crystal structures of Escherichia coli apo-CaiB, as well as its Asp169Ala mutant bound to CoA and to carnitinyl-CoA, have been determined and refined to 1.6, 2.4, and 2.4 A resolution, respectively. CaiB is composed of two identical circular chains that together form an intertwined dimer. Each monomer consists of a large domain, containing a Rossmann fold, and a small domain. The monomer and dimer resemble those of formyl-CoA transferase from Oxalobacter formigenes, as well as E. coli YfdW, a putative type-III CoA transferase of unknown function. The CoA cofactor-binding site is formed at the interface of the large domain of one monomer and the small domain from the second monomer. Most of the protein-CoA interactions are formed with the Rossmann fold domain. While the location of cofactor binding is similar in the three proteins, the specific CoA-protein interactions vary somewhat between CaiB, formyl-CoA transferase, and YfdW. CoA binding results in a change in the relative positions of the large and small domains compared with apo-CaiB. The observed carnitinyl-CoA product in crystals of the CaiB Asp169Ala mutant cocrystallized with crotonoyl-CoA and carnitine could result from (i) a catalytic mechanism involving a ternary enzyme-substrate complex, independent of a covalent anhydride intermediate with Asp169, (ii) a spontaneous reaction of the substrates in solution, followed by binding to the enzyme, or (iii) an involvement of another residue substituting functionally for Asp169, such as Glu23.
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==About this Structure==
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Crystal structure of Escherichia coli crotonobetainyl-CoA: carnitine CoA-transferase (CaiB) and its complexes with CoA and carnitinyl-CoA.,Rangarajan ES, Li Y, Iannuzzi P, Cygler M, Matte A Biochemistry. 2005 Apr 19;44(15):5728-38. PMID:15823031<ref>PMID:15823031</ref>
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1XVV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with CCQ as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XVV OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure of Escherichia coli crotonobetainyl-CoA: carnitine CoA-transferase (CaiB) and its complexes with CoA and carnitinyl-CoA., Rangarajan ES, Li Y, Iannuzzi P, Cygler M, Matte A, Biochemistry. 2005 Apr 19;44(15):5728-38. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15823031 15823031]
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</div>
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<div class="pdbe-citations 1xvv" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Cygler, M.]]
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[[Category: Cygler M]]
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[[Category: Iannuzzi, P.]]
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[[Category: Iannuzzi P]]
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[[Category: Li, Y.]]
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[[Category: Li Y]]
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[[Category: Matte, A.]]
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[[Category: Matte A]]
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[[Category: Rangarajan, E.S.]]
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[[Category: Rangarajan ES]]
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[[Category: CCQ]]
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[[Category: asp mutant]]
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[[Category: caib]]
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[[Category: carnityl-coa]]
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[[Category: coa-transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:22:56 2007''
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Current revision

Crystal Structure of CaiB mutant D169A in complex with carnitinyl-CoA

PDB ID 1xvv

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