1kyq: Difference between revisions

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[[Image:1kyq.png|left|200px]]


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==Met8p: A bifunctional NAD-dependent dehydrogenase and ferrochelatase involved in siroheme synthesis.==
The line below this paragraph, containing "STRUCTURE_1kyq", creates the "Structure Box" on the page.
<StructureSection load='1kyq' size='340' side='right'caption='[[1kyq]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1kyq]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KYQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KYQ FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#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=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
{{STRUCTURE_1kyq|  PDB=1kyq  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kyq OCA], [https://pdbe.org/1kyq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kyq RCSB], [https://www.ebi.ac.uk/pdbsum/1kyq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kyq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MET8_YEAST MET8_YEAST] Catalyzes the conversion of precorrin-2 into siroheme. This reaction consist of the NAD-dependent oxidation of precorrin-2 into sirohydrochlorin and its subsequent ferrochelation into siroheme.<ref>PMID:10051442</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ky/1kyq_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1kyq ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Sirohaem is a tetrapyrrole-derived prosthetic group that is required for the essential assimilation of sulfur and nitrogen into all living systems as part of the sulfite and nitrite reductase systems. The final two steps in the biosynthesis of sirohaem involve a beta-NAD(+)-dependent dehydrogenation of precorrin-2 to generate sirohydrochlorin followed by ferrochelation to yield sirohaem. In Saccharomyces cerevisiae, Met8p is a bifunctional enzyme that carries out both of these reactions. Here, we report the 2.2 A resolution crystal structure of Met8p, which adopts a novel fold that bears no resemblance to the previously determined structures of cobalt- or ferro-chelatases. Analysis of mutant proteins suggests that both catalytic activities share a single active site, and that Asp141 plays an essential role in both dehydrogenase and chelatase processes.


===Met8p: A bifunctional NAD-dependent dehydrogenase and ferrochelatase involved in siroheme synthesis.===
The structure of Saccharomyces cerevisiae Met8p, a bifunctional dehydrogenase and ferrochelatase.,Schubert HL, Raux E, Brindley AA, Leech HK, Wilson KS, Hill CP, Warren MJ EMBO J. 2002 May 1;21(9):2068-75. PMID:11980703<ref>PMID:11980703</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
The line below this paragraph, {{ABSTRACT_PUBMED_11980703}}, adds the Publication Abstract to the page
<div class="pdbe-citations 1kyq" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 11980703 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_11980703}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1KYQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KYQ OCA].
 
==Reference==
The structure of Saccharomyces cerevisiae Met8p, a bifunctional dehydrogenase and ferrochelatase., Schubert HL, Raux E, Brindley AA, Leech HK, Wilson KS, Hill CP, Warren MJ, EMBO J. 2002 May 1;21(9):2068-75. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11980703 11980703]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Brindley AA]]
[[Category: Brindley, A A.]]
[[Category: Hill CP]]
[[Category: Hill, C P.]]
[[Category: Raux E]]
[[Category: Raux, E.]]
[[Category: Schubert HL]]
[[Category: Schubert, H L.]]
[[Category: Warren MJ]]
[[Category: Warren, M J.]]
[[Category: Wilson KS]]
[[Category: Wilson, K S.]]
[[Category: Homodimer]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 11:18:47 2008''

Latest revision as of 11:36, 6 November 2024

Met8p: A bifunctional NAD-dependent dehydrogenase and ferrochelatase involved in siroheme synthesis.Met8p: A bifunctional NAD-dependent dehydrogenase and ferrochelatase involved in siroheme synthesis.

Structural highlights

1kyq is a 3 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MET8_YEAST Catalyzes the conversion of precorrin-2 into siroheme. This reaction consist of the NAD-dependent oxidation of precorrin-2 into sirohydrochlorin and its subsequent ferrochelation into siroheme.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Sirohaem is a tetrapyrrole-derived prosthetic group that is required for the essential assimilation of sulfur and nitrogen into all living systems as part of the sulfite and nitrite reductase systems. The final two steps in the biosynthesis of sirohaem involve a beta-NAD(+)-dependent dehydrogenation of precorrin-2 to generate sirohydrochlorin followed by ferrochelation to yield sirohaem. In Saccharomyces cerevisiae, Met8p is a bifunctional enzyme that carries out both of these reactions. Here, we report the 2.2 A resolution crystal structure of Met8p, which adopts a novel fold that bears no resemblance to the previously determined structures of cobalt- or ferro-chelatases. Analysis of mutant proteins suggests that both catalytic activities share a single active site, and that Asp141 plays an essential role in both dehydrogenase and chelatase processes.

The structure of Saccharomyces cerevisiae Met8p, a bifunctional dehydrogenase and ferrochelatase.,Schubert HL, Raux E, Brindley AA, Leech HK, Wilson KS, Hill CP, Warren MJ EMBO J. 2002 May 1;21(9):2068-75. PMID:11980703[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Raux E, McVeigh T, Peters SE, Leustek T, Warren MJ. The role of Saccharomyces cerevisiae Met1p and Met8p in sirohaem and cobalamin biosynthesis. Biochem J. 1999 Mar 15;338 ( Pt 3):701-8. PMID:10051442
  2. ↑ Schubert HL, Raux E, Brindley AA, Leech HK, Wilson KS, Hill CP, Warren MJ. The structure of Saccharomyces cerevisiae Met8p, a bifunctional dehydrogenase and ferrochelatase. EMBO J. 2002 May 1;21(9):2068-75. PMID:11980703 doi:10.1093/emboj/21.9.2068

1kyq, resolution 2.20Å

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