DIFFERENCES IN THE METAL-ION STRUCTURE BETWEEN SR- AND CA-PROTHROMBIN FRAGMENT-1

被引：18

作者：

SESHADRI, TP ^{[1
]}

SKRZYPCZAKJANKUN, E ^{[1
]}

YIN, M ^{[1
]}

TULINSKY, A ^{[1
]}

机构：

[1] MICHIGAN STATE UNIV,DEPT CHEM,E LANSING,MI 48824

来源：

BIOCHEMISTRY | 1994年 / 33卷 / 05期

关键词：

D O I：

10.1021/bi00171a006

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 structure of Sr-prothrombin fragment 1 has been solved and refined by restrained least-squares methods at 2.5-Angstrom resolution to a crystallographic R value of 0.167. The protein structure is very similar to that of Ca-fragment 1. A polymeric array of five Sr2+ ions separated by about 4.0 Angstrom is buried. among six gamma-carboxyglutamic acid (Gla) residues; three other Sr2+ ions interact with other Gla residues and are located further apart. One of these was not found in the Ca-fragment 1 structure. The coordination of the Sr2+ ions resembles that of Ca2+, but there are some significant differences between them. The most notable is the lack of water coordination with Sr2+ ions and two conformations for Gla 8, which change the coordination of Sr-2 and Sr-3. A hexose moiety of an oligosaccharide was located in the vicinity of Asn101 that was flexibly disordered in Ca-fragment 1. The new Sr2+ ion found may be involved in metal ion phospholipid binding interactions along with Sr-1, and Sr-7, Sr-8.

引用

页码：1087 / 1092

页数：6

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