3CB0

CobR

Summary for 3CB0

• Entry DOI: 10.2210/pdb3cb0/pdb
• Descriptor: 4-HYDROXYPHENYLACETATE 3-MONOOXYGENASE, FLAVIN MONONUCLEOTIDE (3 entities in total)
• Functional Keywords: corrin reductase, cobr, six-stranded anti-parallel beta-barrel, oxidoreductase
• Biological source: Brucella melitensis
• Total number of polymer chains: 4
• Total formula weight: 75901.57

Authors

Lawrence, A.D.,Warren, M.J.,Pickersgill, R.W. (deposition date: 2008-02-21, release date: 2008-03-11, Last modification date: 2024-03-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.6 Å)