2cn6: Difference between revisions
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==About this Structure== | ==About this Structure== | ||
2CN6 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with ZN, CA and GOL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ | 2CN6 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with ZN, CA and GOL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Ferroxidase Ferroxidase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.16.3.1 1.16.3.1]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CN6 OCA]]. | ||
==Reference== | ==Reference== | ||
High-resolution X-ray structures of human apoferritin H-chain mutants correlated with their activity and metal-binding sites., Toussaint L, Bertrand L, Hue L, Crichton RR, Declercq JP, J Mol Biol. 2007 Jan 12;365(2):440-52. Epub 2006 Oct 7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17070541 17070541] | High-resolution X-ray structures of human apoferritin H-chain mutants correlated with their activity and metal-binding sites., Toussaint L, Bertrand L, Hue L, Crichton RR, Declercq JP, J Mol Biol. 2007 Jan 12;365(2):440-52. Epub 2006 Oct 7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17070541 17070541] | ||
[[Category: Ferroxidase]] | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: phosphorylation]] | [[Category: phosphorylation]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:09:23 2007'' | ||
Revision as of 11:04, 30 October 2007
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RECOMBINANT HUMAN H FERRITIN, K86Q AND E107D MUTANT, SOAKED WITH ZN IONS
OverviewOverview
Ferritins are a family of proteins distributed widely in nature. In, bacterial, plant, and animal cells, ferritin appears to serve as a, soluble, bioavailable, and non-toxic form of iron provider. Ferritins from, animal sources are heteropolymers composed of two types of subunit, H and, L, which differ mainly by the presence (H) or absence (L) of active, ferroxidase centres. We report the crystallographic structures of four, human H apoferritin variants at a resolution of up to 1.5 Angstrom., Crystal derivatives using Zn(II) as redox-stable alternative for Fe(II), allows us to characterize the different metal-binding sites. The, ferroxidase centre, which is composed of sites A and B, binds metal with a, preference for the A site. In addition, distinct Zn(II)-binding sites were, found in ... [(full description)]
About this StructureAbout this Structure
2CN6 is a [Single protein] structure of sequence from [Homo sapiens] with ZN, CA and GOL as [ligands]. Active as [Ferroxidase], with EC number [1.16.3.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
High-resolution X-ray structures of human apoferritin H-chain mutants correlated with their activity and metal-binding sites., Toussaint L, Bertrand L, Hue L, Crichton RR, Declercq JP, J Mol Biol. 2007 Jan 12;365(2):440-52. Epub 2006 Oct 7. PMID:17070541
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