1fgj
From Proteopedia
(New page: 200px<br /><applet load="1fgj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fgj, resolution 2.8Å" /> '''X-RAY STRUCTURE OF HY...) |
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| - | [[Image:1fgj.gif|left|200px]]<br /><applet load="1fgj" size=" | + | [[Image:1fgj.gif|left|200px]]<br /><applet load="1fgj" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fgj, resolution 2.8Å" /> | caption="1fgj, resolution 2.8Å" /> | ||
'''X-RAY STRUCTURE OF HYDROXYLAMINE OXIDOREDUCTASE'''<br /> | '''X-RAY STRUCTURE OF HYDROXYLAMINE OXIDOREDUCTASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The 2.8 A crystal structure of hydroxylamine oxidoreductase of a | + | The 2.8 A crystal structure of hydroxylamine oxidoreductase of a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea, is described. Twenty-four haems lie in the centre bottom of the trimeric molecule, localized in four clusters within each monomer. The haem clusters within the trimer are aligned to form a ring that has inlet and outlet sites. The inlet is occupied by a novel haem, P460, and there are two possible outlet sites per monomer formed by paired haems lying within a cavity or cleft on the protein surface. The structure suggests pathways by which electron transfer may occur through the precisely arranged haems and provides a framework for the interpretation of previous and future biochemical and genetic observations. |
==About this Structure== | ==About this Structure== | ||
| - | 1FGJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Nitrosomonas_europaea Nitrosomonas europaea] with HEM and HEC as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Hydroxylamine_oxidase Hydroxylamine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.3.4 1.7.3.4] Full crystallographic information is available from [http:// | + | 1FGJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Nitrosomonas_europaea Nitrosomonas europaea] with <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=HEC:'>HEC</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Hydroxylamine_oxidase Hydroxylamine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.3.4 1.7.3.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FGJ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:38:25 2008'' |
Revision as of 10:38, 21 February 2008
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X-RAY STRUCTURE OF HYDROXYLAMINE OXIDOREDUCTASE
Overview
The 2.8 A crystal structure of hydroxylamine oxidoreductase of a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea, is described. Twenty-four haems lie in the centre bottom of the trimeric molecule, localized in four clusters within each monomer. The haem clusters within the trimer are aligned to form a ring that has inlet and outlet sites. The inlet is occupied by a novel haem, P460, and there are two possible outlet sites per monomer formed by paired haems lying within a cavity or cleft on the protein surface. The structure suggests pathways by which electron transfer may occur through the precisely arranged haems and provides a framework for the interpretation of previous and future biochemical and genetic observations.
About this Structure
1FGJ is a Single protein structure of sequence from Nitrosomonas europaea with and as ligands. Active as Hydroxylamine oxidase, with EC number 1.7.3.4 Full crystallographic information is available from OCA.
Reference
The 2.8 A structure of hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea., Igarashi N, Moriyama H, Fujiwara T, Fukumori Y, Tanaka N, Nat Struct Biol. 1997 Apr;4(4):276-84. PMID:9095195
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