1rtp: Difference between revisions
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|PDB= 1rtp |SIZE=350|CAPTION= <scene name='initialview01'>1rtp</scene>, resolution 2.0Å | |PDB= 1rtp |SIZE=350|CAPTION= <scene name='initialview01'>1rtp</scene>, resolution 2.0Å | ||
|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=1rtp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rtp OCA], [http://www.ebi.ac.uk/pdbsum/1rtp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rtp RCSB]</span> | |||
}} | }} | ||
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[[Category: Santarsiero, B D.]] | [[Category: Santarsiero, B D.]] | ||
[[Category: Sielecki, A R.]] | [[Category: Sielecki, A R.]] | ||
[[Category: calcium-binding protein]] | [[Category: calcium-binding 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 23:32:45 2008'' | ||
Revision as of 23:32, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
REFINED X-RAY STRUCTURE OF RAT PARVALBUMIN, A MAMMALIAN ALPHA-LINEAGE PARVALBUMIN, AT 2.0 A RESOLUTION
OverviewOverview
We present here the X-ray crystal structure of the rat alpha-parvalbumin from fast twitch muscle. This protein (M(r) 11.8 kDa) crystallizes in space group P2(1)2(1)2(1) with unit cell dimensions of a = 34.3 A, b = 55.0 A, c = 156.1 A and three molecules in the asymmetric unit. The protein structure was solved by the molecular replacement method and has been refined to a crystallographic R-factor [formula: see text] of 0.181 for all reflections with I/sigma(I) > or = 2 (I = intensity) between 8.0 and 2.0 A resolution. The molecules located most easily in the molecular replacement rotation function had lower overall thermal motion parameters and higher numbers of intermolecular crystal packing contacts. The overall fold of the polypeptide chain for the rat alpha-parvalbumin is similar to other known parvalbumin structures (root-mean-square deviations in alpha-carbon atom positions range from 0.60 to 0.87 A). There are two Ca(2+)-binding sites in parvalbumins, and there is some evidence for a third ion-binding site, adjacent to the CD site, in the rat species. The level of structural variability among the best-ordered regions of the three independent rat alpha-parvalbumin molecules in the crystallographic asymmetric unit is two to three times higher than the mean coordinate error (0.10 A), indicating flexibility in the molecule. Sequence differences between alpha and beta-lineage parvalbumins result in repacking of the hydrophobic core and some shifts in the protein backbone. The shifts are localized, however, and entire helices do not shift as rigid units.
About this StructureAbout this Structure
1RTP is a Single protein structure of sequence from Rattus rattus. Full crystallographic information is available from OCA.
ReferenceReference
Refined crystal structure of rat parvalbumin, a mammalian alpha-lineage parvalbumin, at 2.0 A resolution., McPhalen CA, Sielecki AR, Santarsiero BD, James MN, J Mol Biol. 1994 Jan 14;235(2):718-32. PMID:8289291
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