3mtw

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[[Image:3mtw.jpg|left|200px]]
 
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==Crystal structure of L-Lysine, L-Arginine carboxypeptidase Cc2672 from Caulobacter Crescentus CB15 complexed with N-methyl phosphonate derivative of L-Arginine==
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The line below this paragraph, containing "STRUCTURE_3mtw", creates the "Structure Box" on the page.
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<StructureSection load='3mtw' size='340' side='right'caption='[[3mtw]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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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'>[[3mtw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caulobacter_vibrioides Caulobacter vibrioides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MTW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MTW 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]] 1.7&#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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=M3R:METHYL+PHOSPHONATED+L-ARGININE'>M3R</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_3mtw| PDB=3mtw | SCENE= }}
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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=3mtw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mtw OCA], [https://pdbe.org/3mtw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mtw RCSB], [https://www.ebi.ac.uk/pdbsum/3mtw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mtw ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9A4Z9_CAUVC Q9A4Z9_CAUVC]
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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/mt/3mtw_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3mtw 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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Two uncharacterized enzymes from the amidohydrolase superfamily belonging to cog1228 were cloned, expressed and purified to homogeneity. The two proteins, Sgx9260c (gi|44242006) and Sgx9260b (gi|44479596), were derived from environmental DNA samples originating from the Sargasso Sea. The catalytic function and substrate profiles for Sgx9260c and Sgx9260b were determined using a comprehensive library of dipeptides and N-acyl derivative of L-amino acids. Sgx9260c catalyzes the hydrolysis of Gly-L-Pro, L-Ala-L-Pro and N-acyl derivatives of L-Pro. The best substrate identified to date is N-acetyl-L-Pro with a value of kcat/Km of 3 x 105 M-1 s-1. Sgx9260b catalyzes the hydrolysis of L-hydrophobic L-Pro dipeptides and N-acyl derivatives of L-Pro. The best substrate identified to date is N-propionyl-L-Pro with a value of kcat/Km of 1 x 105 M-1 s-1. Three dimensional structures of both proteins were determined by X-ray diffraction methods (PDB codes: 3MKV and 3FEQ). These proteins fold as distorted (beta/alpha)8-barrels with two divalent cations in the active site. The structure of Sgx9260c was also determined as a complex with the N-methyl phosphonate derivative of L-Pro (PDB code: 3N2C). In this structure the phosphonate moiety bridges the binuclear metal center and one oxygen atom interacts with His-140. The alpha-carboxylate of the inhibitor interacts with Tyr-231. The proline side chain occupies a small substrate binding cavity formed by residues contributed from the loop that follows beta-strand 7 within the (beta/alpha)8-barrel. A total of 38 other proteins from cog1228 are predicted to have the same substrate profile based on conservation of the substrate binding residues. The structure of an evolutionarily related protein, Cc2672 from Caulobacter crecentus, was determined as a complex with the N-methyl phosphonate derivative of L-arginine (PDB code: 3MTW).
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===Crystal structure of L-Lysine, L-Arginine carboxypeptidase Cc2672 from Caulobacter Crescentus CB15 complexed with N-methyl phosphonate derivative of L-Arginine===
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Functional Identification and Structure Determination of Two Novel Prolidases from cog1228 in the Amidohydrolase Superfamily.,Xiang DF, Patskovsky Y, Xu C, Fedorov A, Fedorov EV, Sisco AA, Sauder JM, Burley SK, Almo S, Raushel FM Biochemistry. 2010 Jul 6. PMID:20604542<ref>PMID:20604542</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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<div class="pdbe-citations 3mtw" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_20604542}}, adds the Publication Abstract to the page
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*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 20604542 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20604542}}
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__TOC__
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</StructureSection>
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==About this Structure==
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3MTW is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Caulobacter_vibrioides Caulobacter vibrioides]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3gnh 3gnh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MTW OCA].
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==Reference==
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<ref group="xtra">PMID:20604542</ref><references group="xtra"/>
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[[Category: Caulobacter vibrioides]]
[[Category: Caulobacter vibrioides]]
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[[Category: Almo, S C.]]
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[[Category: Large Structures]]
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[[Category: Fedorov, A A.]]
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[[Category: Almo SC]]
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[[Category: Fedorov, E V.]]
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[[Category: Fedorov AA]]
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[[Category: Raushel, F M.]]
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[[Category: Fedorov EV]]
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[[Category: Xiang, D F.]]
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[[Category: Raushel FM]]
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[[Category: Hydrolase]]
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[[Category: Xiang DF]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 28 12:31:19 2010''
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Current revision

Crystal structure of L-Lysine, L-Arginine carboxypeptidase Cc2672 from Caulobacter Crescentus CB15 complexed with N-methyl phosphonate derivative of L-Arginine

PDB ID 3mtw

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