3qpi: Difference between revisions

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<StructureSection load='3qpi' size='340' side='right'caption='[[3qpi]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='3qpi' size='340' side='right'caption='[[3qpi]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3qpi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Nitwn Nitwn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QPI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QPI FirstGlance]. <br>
<table><tr><td colspan='2'>[[3qpi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Nitrobacter_winogradskyi_Nb-255 Nitrobacter winogradskyi Nb-255]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QPI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QPI FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Nwi_2442 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=323098 NITWN])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Chlorite_O(2)-lyase Chlorite O(2)-lyase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.49 1.13.11.49] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3qpi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qpi OCA], [https://pdbe.org/3qpi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qpi RCSB], [https://www.ebi.ac.uk/pdbsum/3qpi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qpi ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3qpi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qpi OCA], [https://pdbe.org/3qpi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qpi RCSB], [https://www.ebi.ac.uk/pdbsum/3qpi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qpi ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/Q3SPU6_NITWN Q3SPU6_NITWN]
Chlorite dismutase (Cld) is a unique heme enzyme catalyzing the conversion of ClO(2)(-) to Cl(-) and O(2). Cld is usually found in perchlorate- or chlorate-reducing bacteria but was also recently identified in a nitrite-oxidizing bacterium of the genus Nitrospira. Here we characterized a novel Cld-like protein from the chemolithoautotrophic nitrite oxidizer Nitrobacter winogradskyi which is significantly smaller than all previously known chlorite dismutases. Its three-dimensional (3D) crystal structure revealed a dimer of two identical subunits, which sharply contrasts with the penta- or hexameric structures of other chlorite dismutases. Despite a truncated N-terminal domain in each subunit, this novel enzyme turned out to be a highly efficient chlorite dismutase (K(m) = 90 muM; k(cat) = 190 s(-1); k(cat)/K(m) = 2.1 x 10(6) M(-1) s(-1)), demonstrating a greater structural and phylogenetic diversity of these enzymes than was previously known. Based on comparative analyses of Cld sequences and 3D structures, signature amino acid residues that can be employed to assess whether uncharacterized Cld-like proteins may have a high chlorite-dismutating activity were identified. Interestingly, proteins that contain all these signatures and are phylogenetically closely related to the novel-type Cld of N. winogradskyi exist in a large number of other microbes, including other nitrite oxidizers.
 
Unexpected diversity of chlorite dismutases: a catalytically efficient dimeric enzyme from Nitrobacter winogradskyi.,Mlynek G, Sjoblom B, Kostan J, Fureder S, Maixner F, Gysel K, Furtmuller PG, Obinger C, Wagner M, Daims H, Djinovic-Carugo K J Bacteriol. 2011 May;193(10):2408-17. Epub 2011 Mar 25. PMID:21441524<ref>PMID:21441524</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3qpi" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Nitwn]]
[[Category: Nitrobacter winogradskyi Nb-255]]
[[Category: Daims, H]]
[[Category: Daims H]]
[[Category: Djinovic-Carugo, K]]
[[Category: Djinovic-Carugo K]]
[[Category: Fuereder, S]]
[[Category: Fuereder S]]
[[Category: Furtmueller, P G]]
[[Category: Furtmueller PG]]
[[Category: Kostan, J]]
[[Category: Kostan J]]
[[Category: Maixner, F]]
[[Category: Maixner F]]
[[Category: Mlynek, G]]
[[Category: Mlynek G]]
[[Category: Obinger, O]]
[[Category: Obinger O]]
[[Category: Sjoeblom, B]]
[[Category: Sjoeblom B]]
[[Category: Wagner, M]]
[[Category: Wagner M]]
[[Category: Chlorite]]
[[Category: Cytoplasma]]
[[Category: Oxidoreductase]]
[[Category: Oxygen]]

Latest revision as of 13:48, 21 February 2024

Crystal Structure of Dimeric Chlorite Dismutases from Nitrobacter winogradskyiCrystal Structure of Dimeric Chlorite Dismutases from Nitrobacter winogradskyi

Structural highlights

3qpi is a 2 chain structure with sequence from Nitrobacter winogradskyi Nb-255. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q3SPU6_NITWN

3qpi, resolution 2.10Å

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OCA
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