3CB0

CobR

3CB0 の概要

• エントリーDOI: 10.2210/pdb3cb0/pdb
• 分子名称: 4-HYDROXYPHENYLACETATE 3-MONOOXYGENASE, FLAVIN MONONUCLEOTIDE (3 entities in total)
• 機能のキーワード: corrin reductase, cobr, six-stranded anti-parallel beta-barrel, oxidoreductase
• 由来する生物種: Brucella melitensis
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 75901.57

構造登録者

Lawrence, A.D.,Warren, M.J.,Pickersgill, R.W. (登録日: 2008-02-21, 公開日: 2008-03-11, 最終更新日: 2024-03-13)

主引用文献

Lawrence, A.D.,Deery, E.,McLean, K.J.,Munro, A.W.,Pickersgill, R.W.,Rigby, S.E.,Warren, M.J.
Identification, characterization, and structure/function analysis of a corrin reductase involved in adenosylcobalamin biosynthesis
J.Biol.Chem., 283:10813-10821, 2008

PubMed Abstract: Vitamin B(12), the antipernicious anemia factor, is the cyano derivative of adenosylcobalamin, which is one of nature's most complex coenzymes. Adenosylcobalamin is made along one of two similar yet distinct metabolic pathways, which are referred to as the aerobic and anaerobic routes. The aerobic pathway for cobalamin biosynthesis proceeds via cobalt insertion into a ring-contracted macrocycle, which is closely followed by adenosylation of the cobalt ion. An important prerequisite for adenosylation is the reduction of the centrally chelated metal from Co(II) to a highly nucleophilic Co(I) form. We have cloned a gene, cobR, encoding a biosynthetic enzyme with this co(II)rrin reductase activity from Brucella melitensis. The protein has been overproduced, and the resulting flavoprotein has been purified, characterized, and crystallized and its structure determined to 1.6A resolution. Kinetic and EPR analysis reveals that the enzyme proceeds via a semiquinone form. It is proposed that CobR may interact with the adenosyltransferase to overcome the large thermodynamic barrier required for co(II)rrin reduction.

PubMed: 18263579
DOI: 10.1074/jbc.M710431200

実験手法

X-RAY DIFFRACTION (1.6 Å)