1mr8: Difference between revisions
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|PDB= 1mr8 |SIZE=350|CAPTION= <scene name='initialview01'>1mr8</scene>, resolution 1.9Å | |PDB= 1mr8 |SIZE=350|CAPTION= <scene name='initialview01'>1mr8</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mr8 OCA], [http://www.ebi.ac.uk/pdbsum/1mr8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mr8 RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==Overview== | ||
The structure of human MRP8 in the calcium-bound form was determined at 1.9 A resolution by X-ray crystallography. The structure was initially solved by MAD phasing of an ytterbium-substituted crystal and was refined against data obtained from a Ca(2+)-bound crystal. The dimeric form of MRP8 was stabilized by hydrophobic interactions between mutually wrapped helices. There were two EF-hand motifs per monomer and each EF-hand bound one Ca(2+) with a different affinity [the affinity of the C-terminal EF-hand (EF-2) for Ca(2+) was stronger than that of the N-terminal EF-hand (EF-1)]. Furthermore, replacement with Yb(3+) occurred in the C-terminal EF-hand only, suggesting a more flexible nature for EF-2 than for EF-1. This, combined with previous observations that the helix in EF-2 (helix III) undergoes a large conformational change upon calcium binding, suggests that the C-terminal EF-hand (EF-2) plays a role as a trigger for Ca(2+)-induced conformational change. | The structure of human MRP8 in the calcium-bound form was determined at 1.9 A resolution by X-ray crystallography. The structure was initially solved by MAD phasing of an ytterbium-substituted crystal and was refined against data obtained from a Ca(2+)-bound crystal. The dimeric form of MRP8 was stabilized by hydrophobic interactions between mutually wrapped helices. There were two EF-hand motifs per monomer and each EF-hand bound one Ca(2+) with a different affinity [the affinity of the C-terminal EF-hand (EF-2) for Ca(2+) was stronger than that of the N-terminal EF-hand (EF-1)]. Furthermore, replacement with Yb(3+) occurred in the C-terminal EF-hand only, suggesting a more flexible nature for EF-2 than for EF-1. This, combined with previous observations that the helix in EF-2 (helix III) undergoes a large conformational change upon calcium binding, suggests that the C-terminal EF-hand (EF-2) plays a role as a trigger for Ca(2+)-induced conformational change. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Nishihira, J.]] | [[Category: Nishihira, J.]] | ||
[[Category: Tanaka, I.]] | [[Category: Tanaka, I.]] | ||
[[Category: calcium-binding protein]] | [[Category: calcium-binding protein]] | ||
[[Category: crystal structure]] | [[Category: crystal structure]] | ||
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[[Category: s100 protein]] | [[Category: s100 protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:20:05 2008'' | ||
Revision as of 19:20, 30 March 2008
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| 1mr8, resolution 1.9Å | |||||||||||||
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| Ligands: | CA | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
MIGRATION INHIBITORY FACTOR-RELATED PROTEIN 8 FROM HUMAN
Overview
The structure of human MRP8 in the calcium-bound form was determined at 1.9 A resolution by X-ray crystallography. The structure was initially solved by MAD phasing of an ytterbium-substituted crystal and was refined against data obtained from a Ca(2+)-bound crystal. The dimeric form of MRP8 was stabilized by hydrophobic interactions between mutually wrapped helices. There were two EF-hand motifs per monomer and each EF-hand bound one Ca(2+) with a different affinity [the affinity of the C-terminal EF-hand (EF-2) for Ca(2+) was stronger than that of the N-terminal EF-hand (EF-1)]. Furthermore, replacement with Yb(3+) occurred in the C-terminal EF-hand only, suggesting a more flexible nature for EF-2 than for EF-1. This, combined with previous observations that the helix in EF-2 (helix III) undergoes a large conformational change upon calcium binding, suggests that the C-terminal EF-hand (EF-2) plays a role as a trigger for Ca(2+)-induced conformational change.
About this Structure
1MR8 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The structure of human MRP8, a member of the S100 calcium-binding protein family, by MAD phasing at 1.9 A resolution., Ishikawa K, Nakagawa A, Tanaka I, Suzuki M, Nishihira J, Acta Crystallogr D Biol Crystallogr. 2000 May;56(Pt 5):559-66. PMID:10771424
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