1qnn: Difference between revisions
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[[Image:1qnn.gif|left|200px]]<br /><applet load="1qnn" size=" | [[Image:1qnn.gif|left|200px]]<br /><applet load="1qnn" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1qnn, resolution 1.80Å" /> | caption="1qnn, resolution 1.80Å" /> | ||
'''CAMBIALISTIC SUPEROXIDE DISMUTASE FROM PORPHYROMONAS GINGIVALIS'''<br /> | '''CAMBIALISTIC SUPEROXIDE DISMUTASE FROM PORPHYROMONAS GINGIVALIS'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1QNN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Porphyromonas_gingivalis Porphyromonas gingivalis] with FE as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] Known structural/functional Sites: <scene name='pdbsite=FE1:Metal Binding Site Of Chain A'>FE1</scene>, <scene name='pdbsite=FE2:Metal Binding Site Of Chain B'>FE2</scene>, <scene name='pdbsite=FE3:Metal Binding Site Of Chain C'>FE3</scene> and <scene name='pdbsite=FE4:Metal Binding Site Of Chain D'>FE4</scene>. Full crystallographic information is available from [http:// | 1QNN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Porphyromonas_gingivalis Porphyromonas gingivalis] with <scene name='pdbligand=FE:'>FE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] Known structural/functional Sites: <scene name='pdbsite=FE1:Metal+Binding+Site+Of+Chain+A'>FE1</scene>, <scene name='pdbsite=FE2:Metal+Binding+Site+Of+Chain+B'>FE2</scene>, <scene name='pdbsite=FE3:Metal+Binding+Site+Of+Chain+C'>FE3</scene> and <scene name='pdbsite=FE4:Metal+Binding+Site+Of+Chain+D'>FE4</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QNN OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
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Revision as of 11:01, 3 February 2008
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CAMBIALISTIC SUPEROXIDE DISMUTASE FROM PORPHYROMONAS GINGIVALIS
OverviewOverview
The crystal structure of cambialistic superoxide dismutase (SOD) from, Porphyromonas gingivalis, which exhibits full activity with either Fe or, Mn at the active site, has been determined at 1.8-A resolution by, molecular replacement and refined to a crystallographic R factor of 17.9%, (Rfree 22.3%). The crystals belong to the space group P212121 (a = 75.5 A, b = 102.7 A, c = 99.6 A) with four identical subunits in the asymmetric, unit. Each pair of subunits forms a compact dimer, but not a tetramer, with 222 point symmetry. Each subunit has 191 amino-acid residues most of, which are visible in electron density maps, and consists of seven alpha, helices and one three-stranded antiparallel beta sheet. The metal ion, a 3, : 1 mixture of Fe and Mn, is coordinated with five ligands (His27, His74, His161, Asp157, and water) arranged at the vertices of a trigonal, bipyramid. Although the overall structural features, including the metal, coordination geometry, are similar to those found in other single-metal, containing SODs, P. gingivalis SOD more closely resembles the dimeric, Fe-SODs from Escherichia coli rather than another cambialistic SOD from, Propionibacterium shermanii, which itself is rather similar to other, tetrameric SODs.
About this StructureAbout this Structure
1QNN is a Single protein structure of sequence from Porphyromonas gingivalis with as ligand. Active as Superoxide dismutase, with EC number 1.15.1.1 Known structural/functional Sites: , , and . Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of cambialistic superoxide dismutase from porphyromonas gingivalis., Sugio S, Hiraoka BY, Yamakura F, Eur J Biochem. 2000 Jun;267(12):3487-95. PMID:10848964
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