1l1l

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{{STRUCTURE_1l1l| PDB=1l1l | SCENE= }}
{{STRUCTURE_1l1l| PDB=1l1l | SCENE= }}
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'''CRYSTAL STRUCTURE OF B-12 DEPENDENT (CLASS II) RIBONUCLEOTIDE REDUCTASE'''
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===CRYSTAL STRUCTURE OF B-12 DEPENDENT (CLASS II) RIBONUCLEOTIDE REDUCTASE===
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==Overview==
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Ribonucleotide reductases (RNRs) catalyze the conversion of ribonucleotides to deoxyribonucleotides, an essential step in DNA biosynthesis and repair. Here we present the crystal structure of class II (coenzyme B12-dependent) ribonucleoside triphosphate reductase (RTPR) from Lactobacillus leichmannii in the apo enzyme form and in complex with the B12 analog adeninylpentylcobalamin at 1.75 and 2.0 A resolution, respectively. This monomeric, allosterically regulated class II RNR retains all the key structural features associated with the catalytic and regulatory machinery of oligomeric RNRs. Surprisingly, the dimer interface responsible for effector binding in class I RNR is preserved through a single 130-residue insertion in the class II structure. Thus, L. leichmannii RNR is a paradigm for the simplest structural entity capable of ribonucleotide reduction, a reaction linking the RNA and DNA worlds.
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(as it appears on PubMed at http://www.pubmed.gov), where 11875520 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11875520}}
==About this Structure==
==About this Structure==
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[[Category: 10-stranded alpha-beta barrel]]
[[Category: 10-stranded alpha-beta barrel]]
[[Category: Central finger loop]]
[[Category: Central finger loop]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:26:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:29:44 2008''

Revision as of 08:29, 2 July 2008

Image:1l1l.png

Template:STRUCTURE 1l1l

CRYSTAL STRUCTURE OF B-12 DEPENDENT (CLASS II) RIBONUCLEOTIDE REDUCTASE

Template:ABSTRACT PUBMED 11875520

About this Structure

1L1L is a Single protein structure of sequence from Lactobacillus leichmannii. Full crystallographic information is available from OCA.

Reference

The crystal structure of class II ribonucleotide reductase reveals how an allosterically regulated monomer mimics a dimer., Sintchak MD, Arjara G, Kellogg BA, Stubbe J, Drennan CL, Nat Struct Biol. 2002 Apr;9(4):293-300. PMID:11875520

Page seeded by OCA on Wed Jul 2 11:29:44 2008

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