1j93

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{{Seed}}
 
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[[Image:1j93.png|left|200px]]
 
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==Crystal Structure and Substrate Binding Modeling of the Uroporphyrinogen-III Decarboxylase from Nicotiana tabacum: Implications for the Catalytic Mechanism==
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The line below this paragraph, containing "STRUCTURE_1j93", creates the "Structure Box" on the page.
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<StructureSection load='1j93' size='340' side='right'caption='[[1j93]], [[Resolution|resolution]] 2.30&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'>[[1j93]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Nicotiana_tabacum Nicotiana tabacum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J93 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J93 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]] 2.3&#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=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_1j93| PDB=1j93 | 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=1j93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j93 OCA], [https://pdbe.org/1j93 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j93 RCSB], [https://www.ebi.ac.uk/pdbsum/1j93 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j93 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DCUP_TOBAC DCUP_TOBAC] Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.[HAMAP-Rule:MF_00218]
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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/j9/1j93_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=1j93 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 enzymatic catalysis of many biological processes of life is supported by the presence of cofactors and prosthetic groups originating from the common tetrapyrrole precursor uroporphyrinogen-III. Uroporphyrinogen-III decarboxylase catalyzes its conversion into coproporphyrinogen-III, leading in plants to chlorophyll and heme biosynthesis. Here we report the first crystal structure of a plant (Nicotiana tabacum) uroporphyrinogen-III decarboxylase, together with the molecular modeling of substrate binding in tobacco and human enzymes. Its structural comparison with the homologous human protein reveals a similar catalytic cleft with six invariant polar residues, Arg(32), Arg(36), Asp(82), Ser(214) (Thr in Escherichia coli), Tyr(159), and His(329) (tobacco numbering). The functional relationships obtained from the structural and modeling analyses of both enzymes allowed the proposal for a refined catalytic mechanism. Asp(82) and Tyr(159) seem to be the catalytic functional groups, whereas the other residues may serve in substrate recognition and binding, with Arg(32) steering its insertion. The crystallographic dimer appears to represent the protein dimer under physiological conditions. The dimeric arrangement offers a plausible mechanism at least for the first two (out of four) decarboxylation steps.
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===Crystal Structure and Substrate Binding Modeling of the Uroporphyrinogen-III Decarboxylase from Nicotiana tabacum: Implications for the Catalytic Mechanism===
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Crystal structure and substrate binding modeling of the uroporphyrinogen-III decarboxylase from Nicotiana tabacum. Implications for the catalytic mechanism.,Martins BM, Grimm B, Mock HP, Huber R, Messerschmidt A J Biol Chem. 2001 Nov 23;276(47):44108-16. Epub 2001 Aug 27. PMID:11524417<ref>PMID:11524417</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_11524417}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1j93" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 11524417 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11524417}}
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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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1J93 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Nicotiana_tabacum Nicotiana tabacum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J93 OCA].
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==Reference==
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<ref group="xtra">PMID:11524417</ref><references group="xtra"/>
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[[Category: Nicotiana tabacum]]
[[Category: Nicotiana tabacum]]
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[[Category: Uroporphyrinogen decarboxylase]]
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[[Category: Grimm B]]
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[[Category: Grimm, B.]]
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[[Category: Huber R]]
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[[Category: Huber, R.]]
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[[Category: Martins BM]]
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[[Category: Martins, B M.]]
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[[Category: Messerschmidt A]]
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[[Category: Messerschmidt, A.]]
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[[Category: Mock H-P]]
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[[Category: Mock, H P.]]
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[[Category: Beta barrel]]
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[[Category: Crystallographic dimer]]
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[[Category: Plastidial enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 04:10:53 2009''
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Current revision

Crystal Structure and Substrate Binding Modeling of the Uroporphyrinogen-III Decarboxylase from Nicotiana tabacum: Implications for the Catalytic Mechanism

PDB ID 1j93

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