PROKARYOTIC CALCIUM-BINDING PROTEIN OF THE CALMODULIN SUPERFAMILY - CALCIUM-BINDING TO A SACCHAROPOLYSPORA-ERYTHRAEA 20 KDA PROTEIN

被引：21

作者：

BYLSMA, N

DRAKENBERG, T

ANDERSSON, I

LEADLAY, PF

FORSEN, S

机构：

[1] UNIV LUND,CTR CHEM,POB 124,S-22100 LUND,SWEDEN

[2] UNIV CAMBRIDGE,DEPT BIOCHEM,CAMBRIDGE CTR MOLEC RECOGNIT,CAMBRIDGE CB2 1QW,ENGLAND

来源：

FEBS LETTERS | 1992年 / 299卷 / 01期

基金：

英国惠康基金;

关键词：

CALCIUM BINDING PROTEIN; PROKARYOTIC; SACCHAROPOLYSPORA-ERYTHRAEA; NMR; CALCIUM AFFINITY;

D O I：

10.1016/0014-5793(92)80096-Y

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The EF-hand calcium-binding protein from Saccharopolyspora erythraea has been shown, using Cd-113 NMR, to possess three Cd2+-ion binding sites. This indicates that of the four EF-hand motifs in the molecule, one (probably site 2) is unable to bind Cd2+-ions. Data from the titration of the protein with Ca2+, in the presence of Quin2, were fitted to a curve calculated on the assumption that the protein contains three high affinity Ca2+ binding sites, two of which (pK1 = 8.0, pK2 = 9.0) are strongly cooperative, and one single site (pK3 = 7.5). Preliminary H-1 NMR experiments indicate marked structural changes upon Ca2+-binding.

引用

页码：44 / 47

页数：4

共 16 条

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