1cdp: Difference between revisions

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[[Image:1cdp.gif|left|200px]]<br /><applet load="1cdp" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1cdp.gif|left|200px]]<br /><applet load="1cdp" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1cdp, resolution 1.6Å" />

'''RESTRAINED LEAST SQUARES REFINEMENT OF NATIVE (CALCIUM) AND CADMIUM-SUBSTITUTED CARP PARVALBUMIN USING X-RAY CRYSTALLOGRAPHIC DATA AT 1.6-ANGSTROMS RESOLUTION'''<br />

==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.

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 [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cyprinus_carpio Cyprinus carpio] with CD and ACE as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1CDP OCA].

1CDP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cyprinus_carpio Cyprinus carpio] with <scene name='pdbligand=CD:'>CD</scene> and <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CDP OCA].

==Reference==

Line 13:

[[Category: Cyprinus carpio]]

[[Category: Single protein]]

[[Category: Amma, E.L.]]

[[Category: Amma, E L.]]

[[Category: Kretsinger, R.H.]]

[[Category: Kretsinger, R H.]]

[[Category: Swain, A.L.]]

[[Category: Swain, A L.]]

[[Category: ACE]]

[[Category: CD]]

[[Category: calcium binding]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:04:59 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1cdp.gif|left|200px]]<br /><applet load="1cdp" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1cdp.gif|left|200px]]<br /><applet load="1cdp" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1cdp, resolution 1.6&Aring;" />
 '''RESTRAINED LEAST SQUARES REFINEMENT OF NATIVE (CALCIUM) AND CADMIUM-SUBSTITUTED CARP PARVALBUMIN USING X-RAY CRYSTALLOGRAPHIC DATA AT 1.6-ANGSTROMS RESOLUTION'''<br />
 ==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.
+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==
-CDP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cyprinus_carpio Cyprinus carpio] with CD and ACE as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CDP OCA].
+CDP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cyprinus_carpio Cyprinus carpio] with <scene name='pdbligand=CD:'>CD</scene> and <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CDP OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Cyprinus carpio]]
 [[Category: Single protein]]
-[[Category: Amma, E.L.]]
+[[Category: Amma, E L.]]
-[[Category: Kretsinger, R.H.]]
+[[Category: Kretsinger, R H.]]
-[[Category: Swain, A.L.]]
+[[Category: Swain, A L.]]
 [[Category: ACE]]
 [[Category: CD]]
 [[Category: calcium binding]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:22:21 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:04:59 2008''