3bpb

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{{Seed}}
 
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[[Image:3bpb.png|left|200px]]
 
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==Crystal structure of the dimethylarginine dimethylaminohydrolase H162G adduct with S-methyl-L-thiocitrulline==
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The line below this paragraph, containing "STRUCTURE_3bpb", creates the "Structure Box" on the page.
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<StructureSection load='3bpb' size='340' side='right'caption='[[3bpb]], [[Resolution|resolution]] 2.81&Aring;' 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'>[[3bpb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BPB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BPB 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">X-ray diffraction, [[Resolution|Resolution]] 2.81&#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=SMZ:N~5~-[(E)-IMINO(METHYLSULFANYL)METHYL]-L-ORNITHINE'>SMZ</scene></td></tr>
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{{STRUCTURE_3bpb| PDB=3bpb | 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=3bpb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bpb OCA], [https://pdbe.org/3bpb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bpb RCSB], [https://www.ebi.ac.uk/pdbsum/3bpb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bpb ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DDAH_PSEAE DDAH_PSEAE] Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS.
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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/bp/3bpb_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=3bpb 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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Many enzymes in the pentein superfamily use a transient covalent intermediate in their catalytic mechanisms. Here we trap and determine the structure of a stable covalent adduct that mimics this intermediate using a mutant dimethylarginine dimethylaminohydrolase and an alternative substrate. The interactions observed between the enzyme and trapped adduct suggest an altered angle of attack between the nucleophiles of the first and second half-reactions of normal catalysis. The stable covalent adduct is also capable of further reaction. Addition of imidazole rescues the original hydrolytic activity. Notably, addition of other amines instead yields substituted arginine products, which arise from partitioning of the intermediate into the evolutionarily related amidinotransferase reaction pathway. The enzyme provides both selectivity and catalysis for the amidinotransferase reaction, underscoring commonalities among the reaction pathways in this mechanistically diverse enzyme superfamily. The promiscuous partitioning of this intermediate may also help to illuminate the evolutionary history of these enzymes.
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===Crystal structure of the dimethylarginine dimethylaminohydrolase H162G adduct with S-methyl-L-thiocitrulline===
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Promiscuous partitioning of a covalent intermediate common in the pentein superfamily.,Linsky TW, Monzingo AF, Stone EM, Robertus JD, Fast W Chem Biol. 2008 May;15(5):467-75. PMID:18482699<ref>PMID:18482699</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_18482699}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3bpb" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 18482699 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18482699}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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3BPB is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BPB OCA].
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==Reference==
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<ref group="xtra">PMID:18482699</ref><references group="xtra"/>
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[[Category: Dimethylargininase]]
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[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
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[[Category: Fast, W.]]
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[[Category: Fast W]]
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[[Category: Linsky, T W.]]
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[[Category: Linsky TW]]
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[[Category: Monzingo, A F.]]
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[[Category: Monzingo AF]]
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[[Category: Robertus, J D.]]
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[[Category: Robertus JD]]
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[[Category: Stone, E M.]]
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[[Category: Stone EM]]
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[[Category: Enzyme adduct]]
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[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 00:56:25 2009''
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Current revision

Crystal structure of the dimethylarginine dimethylaminohydrolase H162G adduct with S-methyl-L-thiocitrulline

PDB ID 3bpb

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