Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1F4O

CRYSTAL STRUCTURE OF GRANCALCIN WITH BOUND CALCIUM

Summary for 1F4O
Entry DOI10.2210/pdb1f4o/pdb
Related1F4Q
DescriptorGRANCALCIN, CALCIUM ION (3 entities in total)
Functional Keywordspenta-ef-hand protein, calcium binding protein, metal transport
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm: P28676
Total number of polymer chains2
Total formula weight37528.47
Authors
Jia, J.,Han, Q.,Borregaard, N.,Lollike, K.,Cygler, M. (deposition date: 2000-06-08, release date: 2000-09-27, Last modification date: 2024-02-07)
Primary citationJia, J.,Han, Q.,Borregaard, N.,Lollike, K.,Cygler, M.
Crystal structure of human grancalcin, a member of the penta-EF-hand protein family.
J.Mol.Biol., 300:1271-1281, 2000
Cited by
PubMed Abstract: Grancalcin is a Ca(2+)-binding protein expressed at high level in neutrophils. It belongs to the PEF family, proteins containing five EF-hand motifs and which are known to associate with membranes in Ca(2+)-dependent manner. Prototypic members of this family are Ca(2+)-binding domains of calpain. Our recent finding that grancalcin interacts with L-plastin, a protein known to have actin bundling activity, suggests that grancalcin may play a role in regulation of adherence and migration of neutrophils. The structure of human grancalcin has been determined at 1.9 A resolution in the absence of calcium (R-factor of 0.212 and R-free of 0.249) and at 2. 5 A resolution in the presence of calcium (R-factor of 0.226 and R-free of 0.281). The molecule is predominantly alpha-helical: it contains eight alpha-helices and only two short stretches of two-stranded beta-sheets between the loops of paired EF-hands. Grancalcin forms dimers through the association of the unpaired EF5 hands in a manner similar to that observed in calpain, confirming this mode of association as a paradigm for the PEF family. Only one Ca(2+) was found per dimer under crystallization conditions that included CaCl(2). This cation binds to EF3 in one molecule, while this site in the second molecule of the dimer is unoccupied. This unoccupied site shows higher mobility. The structure determined in the presence of calcium, although does not represent a fully Ca(2+)-loaded form, suggests that calcium induces rather small conformational rearrangements. Comparison with calpain suggests further that the relatively small magnitude of conformational changes invoked by calcium alone may be a characteristic feature of the PEF family. Moreover, the largest differences are localized to the EF1, thus supporting the notion that calcium signaling occurs through this portion of the molecule and that it may involve the N-terminal Gly/Pro rich segment. Electrostatic potential distribution shows significant differences between grancalcin and calpain domain VI demonstrating their distinct character.
PubMed: 10903868
DOI: 10.1006/jmbi.2000.3925
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

239492

數據於2025-07-30公開中

PDB statisticsPDBj update infoContact PDBjnumon