1zrr

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{{Seed}}
 
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[[Image:1zrr.png|left|200px]]
 
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==Residual Dipolar Coupling Refinement of Acireductone Dioxygenase from Klebsiella==
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The line below this paragraph, containing "STRUCTURE_1zrr", creates the "Structure Box" on the page.
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<StructureSection load='1zrr' size='340' side='right'caption='[[1zrr]]' 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'>[[1zrr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_oxytoca Klebsiella oxytoca]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1m4o 1m4o]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZRR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZRR 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
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{{STRUCTURE_1zrr| PDB=1zrr | 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=1zrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zrr OCA], [https://pdbe.org/1zrr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zrr RCSB], [https://www.ebi.ac.uk/pdbsum/1zrr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zrr ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MTND_KLEOX MTND_KLEOX] Catalyzes 2 different reactions between oxygene and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway.<ref>PMID:8407993</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/zr/1zrr_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=1zrr 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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Acireductone dioxygenase (ARD) from Klebsiella ATCC 8724 is a metalloenzyme that is capable of catalyzing different reactions with the same substrates (acireductone and O2) depending upon the metal bound in the active site. A model for the solution structure of the paramagnetic Ni2+-containing ARD has been refined using residual dipolar couplings (RDCs) measured in two media. Additional dihedral restraints based on chemical shift (TALOS) were included in the refinement, and backbone structure in the vicinity of the active site was modeled from a crystallographic structure of the mouse homolog of ARD. The incorporation of residual dipolar couplings into the structural refinement alters the relative orientations of several structural features significantly, and improves local secondary structure determination. Comparisons between the solution structures obtained with and without RDCs are made, and structural similarities and differences between mouse and bacterial enzymes are described. Finally, the biological significance of these differences is considered.
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===Residual Dipolar Coupling Refinement of Acireductone Dioxygenase from Klebsiella===
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A refined model for the structure of acireductone dioxygenase from Klebsiella ATCC 8724 incorporating residual dipolar couplings.,Pochapsky TC, Pochapsky SS, Ju T, Hoefler C, Liang J J Biomol NMR. 2006 Feb;34(2):117-27. PMID:16518698<ref>PMID:16518698</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_16518698}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1zrr" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16518698 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16518698}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1ZRR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Klebsiella_oxytoca Klebsiella oxytoca]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1m4o 1m4o]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZRR OCA].
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==Reference==
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A refined model for the structure of acireductone dioxygenase from Klebsiella ATCC 8724 incorporating residual dipolar couplings., Pochapsky TC, Pochapsky SS, Ju T, Hoefler C, Liang J, J Biomol NMR. 2006 Feb;34(2):117-27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16518698 16518698]
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Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae., Pochapsky TC, Pochapsky SS, Ju T, Mo H, Al-Mjeni F, Maroney MJ, Nat Struct Biol. 2002 Dec;9(12):966-72. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12402029 12402029]
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Mechanistic studies of two dioxygenases in the methionine salvage pathway of Klebsiella pneumoniae., Dai Y, Pochapsky TC, Abeles RH, Biochemistry. 2001 May 29;40(21):6379-87. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11371200 11371200]
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[[Category: Klebsiella oxytoca]]
[[Category: Klebsiella oxytoca]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Hoefler, C.]]
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[[Category: Hoefler C]]
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[[Category: Ju, T.]]
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[[Category: Ju T]]
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[[Category: Liang, J.]]
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[[Category: Liang J]]
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[[Category: Pochapsky, S S.]]
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[[Category: Pochapsky SS]]
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[[Category: Pochapsky, T C.]]
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[[Category: Pochapsky TC]]
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[[Category: Beta helix]]
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[[Category: Cupin]]
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[[Category: Methionine salvage]]
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[[Category: Nickel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:49:57 2008''
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Current revision

Residual Dipolar Coupling Refinement of Acireductone Dioxygenase from Klebsiella

PDB ID 1zrr

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