2j5w
From Proteopedia
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==Overview== | ==Overview== | ||
The three-dimensional molecular structure of human serum ceruloplasmin has, been reinvestigated using X-ray synchrotron data collected at 100 K from a, crystal frozen to liquid-nitrogen temperature. The resulting model, with, an increase in resolution from 3.1 to 2.8 A, gives an overall improvement, of the molecular structure, in particular the side chains. In addition, it, enables the clear definition of previously unidentified Ca2+-binding and, Na+-binding sites. The Ca2+ cation is located in domain 1 in a, configuration very similar to that found in the activated bovine factor, Va. The Na+ sites appear to play a structural role in providing rigidity, to the three protuberances on the top surface of the molecule. These, features probably help to steer substrates towards the mononuclear copper, sites prior to their oxidation and to restrict the size of the approaching, substrate. The trinuclear copper centre appears to differ from the, room-temperature structure in that a dioxygen moiety is bound in a similar, way to that found in the endospore coat protein CotA from Bacillus, subtilis. | The three-dimensional molecular structure of human serum ceruloplasmin has, been reinvestigated using X-ray synchrotron data collected at 100 K from a, crystal frozen to liquid-nitrogen temperature. The resulting model, with, an increase in resolution from 3.1 to 2.8 A, gives an overall improvement, of the molecular structure, in particular the side chains. In addition, it, enables the clear definition of previously unidentified Ca2+-binding and, Na+-binding sites. The Ca2+ cation is located in domain 1 in a, configuration very similar to that found in the activated bovine factor, Va. The Na+ sites appear to play a structural role in providing rigidity, to the three protuberances on the top surface of the molecule. These, features probably help to steer substrates towards the mononuclear copper, sites prior to their oxidation and to restrict the size of the approaching, substrate. The trinuclear copper centre appears to differ from the, room-temperature structure in that a dioxygen moiety is bound in a similar, way to that found in the endospore coat protein CotA from Bacillus, subtilis. | ||
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| + | ==Disease== | ||
| + | Known diseases associated with this structure: Cerebellar ataxia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=117700 117700]], Hemosiderosis, systemic, due to aceruloplasminemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=117700 117700]], Hypoceruloplasminemia, hereditary OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=117700 117700]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: transport]] | [[Category: transport]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:52:07 2007'' |
Revision as of 20:45, 12 November 2007
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CERULOPLASMIN REVISITED: STRUCTURAL AND FUNCTIONAL ROLES OF VARIOUS METAL CATION BINDING SITES
Contents |
Overview
The three-dimensional molecular structure of human serum ceruloplasmin has, been reinvestigated using X-ray synchrotron data collected at 100 K from a, crystal frozen to liquid-nitrogen temperature. The resulting model, with, an increase in resolution from 3.1 to 2.8 A, gives an overall improvement, of the molecular structure, in particular the side chains. In addition, it, enables the clear definition of previously unidentified Ca2+-binding and, Na+-binding sites. The Ca2+ cation is located in domain 1 in a, configuration very similar to that found in the activated bovine factor, Va. The Na+ sites appear to play a structural role in providing rigidity, to the three protuberances on the top surface of the molecule. These, features probably help to steer substrates towards the mononuclear copper, sites prior to their oxidation and to restrict the size of the approaching, substrate. The trinuclear copper centre appears to differ from the, room-temperature structure in that a dioxygen moiety is bound in a similar, way to that found in the endospore coat protein CotA from Bacillus, subtilis.
Disease
Known diseases associated with this structure: Cerebellar ataxia OMIM:[117700], Hemosiderosis, systemic, due to aceruloplasminemia OMIM:[117700], Hypoceruloplasminemia, hereditary OMIM:[117700]
About this Structure
2J5W is a Single protein structure of sequence from Homo sapiens with NAG, CA, NA, CU, O, OXY 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.
Reference
Ceruloplasmin revisited: structural and functional roles of various metal cation-binding sites., Bento I, Peixoto C, Zaitsev VN, Lindley PF, Acta Crystallogr D Biol Crystallogr. 2007 Feb;63(Pt 2):240-8. Epub 2007, Jan 16. PMID:17242517
Page seeded by OCA on Mon Nov 12 22:52:07 2007
Categories: Ferroxidase | Homo sapiens | Single protein | Bento, I. | Lindley, P.F. | Peixoto, C. | Zaitsev, V.N. | CA | CU | GOL | NA | NAG | O | OXY | Ceruloplasmin | Copper | Copper transport | Glycoprotein | Ion transport | Metal-binding | Multi-copper oxidase | Oxidoreductase | Plasma protein | Polymorphism | Transport
