2j5w
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The three-dimensional molecular structure of human serum ceruloplasmin has | + | 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== | ==Disease== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bento, I.]] | [[Category: Bento, I.]] | ||
| - | [[Category: Lindley, P | + | [[Category: Lindley, P F.]] |
[[Category: Peixoto, C.]] | [[Category: Peixoto, C.]] | ||
| - | [[Category: Zaitsev, V | + | [[Category: Zaitsev, V N.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: CU]] | [[Category: CU]] | ||
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[[Category: transport]] | [[Category: transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:59:35 2008'' |
Revision as of 15:59, 21 February 2008
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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 , , , , , and as ligands. Active as Ferroxidase, with EC number 1.16.3.1 Known structural/functional Site: . 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 Thu Feb 21 17:59:35 2008
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
