The structure and function of the 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase from Haemophilus influenzae

被引：51

作者：

Hennig, M ^{[1
]}

Dale, GE ^{[1
]}

D'Arcy, A ^{[1
]}

Danel, F ^{[1
]}

Fischer, S ^{[1
]}

Gray, CP ^{[1
]}

Jolidon, S ^{[1
]}

Müller, F ^{[1
]}

Page, MGP ^{[1
]}

Pattison, P ^{[1
]}

Oefner, C ^{[1
]}

机构：

[1] F Hoffmann La Roche & Co Ltd, Pharma Preclin Res, CH-4070 Basel, Switzerland

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1999年 / 287卷 / 02期

关键词：

HPPK; pterin; pyrophosphokinase; MAD; X-ray structure;

D O I：

10.1006/jmbi.1999.2623

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 gene encoding the 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase of Haemophilus influenzae has been cloned and expressed in Escherichia coli. A complex of the purified protein with a substrate analog has been crystallized and its structure solved by multiple anomalous dispersion using phase information obtained from a single crystal of selenomethione-labeled protein. The enzyme folds into a four-stranded antiparallel beta-sheet flanked on one side by two alpha-helices and on the other by three consecutive alpha-helices, giving a novel beta(1)alpha(1)beta(2)beta(3)alpha(2)beta(4)alpha(3)alpha(4)alpha(5) polypeptide topology. The three-dimensional structure of a binary complex has been refined at 2.1 Angstrom resolution. The location of the substrate analog and a sulfate ion gives important insight into the molecular mechanism of the enzyme. (C) 1999 Academic Press.

引用

页码：211 / 219

页数：9

共 45 条

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