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1a4v
From Proteopedia
| 1a4v, resolution 1.80Å () | |||||||||
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| Sites: | , , and | ||||||||
| Ligands: | |||||||||
| Activity: | Lactose synthase, with EC number 2.4.1.22 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
ALPHA-LACTALBUMIN
The high-resolution X-ray crystal structure of human alpha-lactalbumin (at 1.8 A) in the presence of an elevated level of calcium reveals a new secondary calcium binding site, 7.9 A away from the primary calcium binding site known in all alpha-lactalbumin structures so far. The new calcium binding site is different from the zinc and sulfate binding sites [Ren, J., et al. (1993) J. Biol. Chem. 268, 19292-19298] but shares common features with the manganese binding site as described by Gerkin [Gerkin, T. A. (1984) Biochemistry 23, 4688-4697]. The proximity of the manganese and calcium binding region and the location of the functional site on one side of the charged surface of the alpha-lactalbumin molecule suggest that these binding sites might play a role in the formation of the lactose synthase complex.
Structural evidence for the presence of a secondary calcium binding site in human alpha-lactalbumin., Chandra N, Brew K, Acharya KR, Biochemistry. 1998 Apr 7;37(14):4767-72. PMID:9537992
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1a4v is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Chandra N, Brew K, Acharya KR. Structural evidence for the presence of a secondary calcium binding site in human alpha-lactalbumin. Biochemistry. 1998 Apr 7;37(14):4767-72. PMID:9537992 doi:10.1021/bi973000t
- Chaudhuri TK, Arai M, Terada TP, Ikura T, Kuwajima K. Equilibrium and kinetic studies on folding of the authentic and recombinant forms of human alpha-lactalbumin by circular dichroism spectroscopy. Biochemistry. 2000 Dec 19;39(50):15643-51. PMID:11112553
