Structure of ferric soybean leghemoglobin a nicotinate at 2.3 angstrom resolution

被引：22

作者：

Ellis, PJ ^{[1
]}

Appleby, CA ^{[1
]}

Guss, JM ^{[1
]}

Hunter, WN ^{[1
]}

Ollis, DL ^{[1
]}

Freeman, HC ^{[1
]}

机构：

[1] CSIRO,DIV PLANT IND,CANBERRA,ACT 2601,AUSTRALIA

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1997年 / 53卷

关键词：

D O I：

10.1107/S0907444997000292

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Soybean leghemoglobin a is a small (16 kDa) protein facilitating the transport of O-2 to respiring N-2-fixing bacteria at low free-O-2 tension. The crystal structure of soybean ferric leghemoglobin a nicotinate has been refined at 2.3 Angstrom resolution. The final R factor is 15.8% for 6877 reflections between 6.0 and 2.3 Angstrom. The structure of soybean leghemoglobin a (143 residues) is closely similar to that of lupin leghemoglobin II (153 residues), the proteins having 82 identical residues when the sequences are aligned. The new structure provides support for the conclusion that the unique properties of leghemoglobin arise principally from a heme pocket considerably larger and more flexible than that of myoglobin, a strongly ruffled heme group, and a proximal histidine orientation more favourable to ligand binding.

引用

页码：302 / 310

页数：9

共 34 条

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[2]

APPLEBY CA, 1992, SCI PROG, V76, P365

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