1cdp
From Proteopedia
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| - | [[Image:1cdp.gif|left|200px]] | + | [[Image:1cdp.gif|left|200px]] |
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| - | '''RESTRAINED LEAST SQUARES REFINEMENT OF NATIVE (CALCIUM) AND CADMIUM-SUBSTITUTED CARP PARVALBUMIN USING X-RAY CRYSTALLOGRAPHIC DATA AT 1.6-ANGSTROMS RESOLUTION''' | + | {{Structure |
| + | |PDB= 1cdp |SIZE=350|CAPTION= <scene name='initialview01'>1cdp</scene>, resolution 1.6Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> and <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''RESTRAINED LEAST SQUARES REFINEMENT OF NATIVE (CALCIUM) AND CADMIUM-SUBSTITUTED CARP PARVALBUMIN USING X-RAY CRYSTALLOGRAPHIC DATA AT 1.6-ANGSTROMS RESOLUTION''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CDP is a [ | + | 1CDP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Cyprinus_carpio Cyprinus carpio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CDP OCA]. |
==Reference== | ==Reference== | ||
| - | Restrained least squares refinement of native (calcium) and cadmium-substituted carp parvalbumin using X-ray crystallographic data at 1.6-A resolution., Swain AL, Kretsinger RH, Amma EL, J Biol Chem. 1989 Oct 5;264(28):16620-8. PMID:[http:// | + | Restrained least squares refinement of native (calcium) and cadmium-substituted carp parvalbumin using X-ray crystallographic data at 1.6-A resolution., Swain AL, Kretsinger RH, Amma EL, J Biol Chem. 1989 Oct 5;264(28):16620-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2777802 2777802] |
[[Category: Cyprinus carpio]] | [[Category: Cyprinus carpio]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: calcium binding]] | [[Category: calcium binding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:23:03 2008'' |
Revision as of 08:23, 20 March 2008
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| , resolution 1.6Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
RESTRAINED LEAST SQUARES REFINEMENT OF NATIVE (CALCIUM) AND CADMIUM-SUBSTITUTED CARP PARVALBUMIN USING X-RAY CRYSTALLOGRAPHIC DATA AT 1.6-ANGSTROMS RESOLUTION
Overview
Carp parvalbumin coordinates calcium through one carbonyl oxygen atom and the oxygen-containing side chains of 5 amino acid residues, or 4 residues and a water molecule, in a helix-loop-helix structural motif. Other calcium-binding proteins, including calmodulin and troponin C, also possess this unique calcium-binding design, which is designated EF-hand or calmodulin fold. Parvalbumin has two such sites, labeled CD and EF. Each of the calcium-binding sites of refined structures of proteins belonging to this group has a 7-oxygen coordination sphere except those of the structure of parvalbumin as it was reported in 1975. This structure had been refined at 1.9 A using difference Fourier techniques on film data. The CD site appeared to be 6-coordinate and the EF site 8-coordinate. Results of NMR experiments using 113Cd-substituted parvalbumin, however, indicate that the sites are similar to one another with coordination number greater than 6. To resolve the inconsistency between crystallographic and NMR results, 1.6 A area detector data was collected for native and cadmium-substituted parvalbumin; the structures have been refined to R factors of 18.7% and 16.4%, respectively, with acceptable geometry and low errors in atomic coordinates. Differences between the parvalbumin structure described in 1975 and the present structure are addressed, including the discovery of 7-coordination for both the CD and EF sites.
About this Structure
1CDP is a Single protein structure of sequence from Cyprinus carpio. Full crystallographic information is available from OCA.
Reference
Restrained least squares refinement of native (calcium) and cadmium-substituted carp parvalbumin using X-ray crystallographic data at 1.6-A resolution., Swain AL, Kretsinger RH, Amma EL, J Biol Chem. 1989 Oct 5;264(28):16620-8. PMID:2777802
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