Structural basis for nick recognition by a minimal pluripotent DNA ligase.

Structural basis for nick recognition by a minimal pluripotent DNA ligase. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Structural basis for nick recognition by a minimal pluripotent DNA ligase. Abstract Text:

Pravin A Nair,Jayakrishnan Nandakumar,Paul Smith,Mark Odell,Christopher D Lima,Stewart Shuman,

Chlorella virus DNA ligase, the smallest eukaryotic ligase known, has pluripotent biological activity and an intrinsic nick-sensing function, despite having none of the accessory domains found in cellular ligases. A 2.3-A crystal structure of the Chlorella virus ligase-AMP intermediate bound to duplex DNA containing a 3'-OH-5'-PO4 nick reveals a new mode of DNA envelopment, in which a short surface loop emanating from the OB domain forms a beta-hairpin 'latch' that inserts into the DNA major groove flanking the nick. A network of interactions with the 3'-OH and 5'-PO4 termini in the active site illuminates the DNA adenylylation mechanism and the crucial roles of AMP in nick sensing and catalysis. Addition of a divalent cation triggered nick sealing in crystallo, establishing that the nick complex is a bona fide intermediate in the DNA repair pathway.

Structural basis for nick recognition by a minimal pluripotent DNA ligase. Publishing Authors By Initials

PA Nair,J Nandakumar,P Smith,M Odell,CD Lima,S Shuman,

For similar proteins: viral proteins research abstracts see: proteins: viral proteins research

PUBMED ID PMID:

MEDLINE DATE:

Structural basis for nick recognition by a minimal pluripotent DNA ligase. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Nature structural & molecular biology

VOLUME: 14

Page Numbers: 770-8

Journal Abbreviation: Nat. Struct. Mol. Biol.

ISSN: 1545-9993

DAY: 8

MONTH: 07

YEAR: 2007

Structural basis for nick recognition by a minimal pluripotent DNA ligase. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 101186374

Structural basis for nick recognition by a minimal pluripotent DNA ligase. Keywords Mesh Terms:

KEYWORDS: Viral Proteins

MESH TERMS: physiology

Chemical & Substance for Abstract: Structural basis for nick recognition by a minimal pluripotent DNA ligase. Information

Substance Name: DNA Ligases

Registry Number: EC 6.5.1.-

Grant and Affiliation Information for Structural basis for nick recognition by a minimal pluripotent DNA ligase.

AFFILIATION: Molecular Biology and Structural Biology Programs, Sloan-Kettering Institute, New York, New York 10021, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: GM63611

ACRONYM: GM

MEDLINETA: Nat Struct Mol Biol

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Structural basis for nick recognition by a minimal pluripotent DNA ligase Related Publications

• An oxygen-humidity-aerosol unit for infants.
• Biochemical and genetic analysis of RNA cap guanine-N2 methyltransferases from Giardia lamblia and Schizosaccharomyces pombe.
• Characterization of Agrobacterium tumefaciens DNA ligases C and D.
• Characterization of the 2',3' cyclic phosphodiesterase activities of Clostridium thermocellum polynucleotide kinase-phosphatase and bacteriophage lambda phosphatase.
• Deinococcus radiodurans RNA ligase exemplifies a novel ligase clade with a distinctive N-terminal module that is important for 5'-PO4 nick sealing and ligase adenylylation but dispensable for phosphodiester formation at an adenylylated nick.
• Host cell-dependent secretion and translocation of the LepA and LepB effectors of Legionella pneumophila.
• Identification of novel antipoxviral agents: mitoxantrone inhibits vaccinia virus replication by blocking virion assembly.
• Incidence and prevalence: proper use.
• Last stop on the road to repair: structure of E. coli DNA ligase bound to nicked DNA-adenylate.
• MR imaging in clinically suspected brachial plexus tumor.
• Mammalian 2',3' cyclic nucleotide phosphodiesterase (CNP) can function as a tRNA splicing enzyme in vivo.
• Mutational analysis of Encephalitozoon cuniculi mRNA cap (guanine-N7) methyltransferase, structure of the enzyme bound to sinefungin, and evidence that cap methyltransferase is the target of sinefungin's antifungal activity.
• Mycobacterial UvrD1 is a Ku-dependent DNA helicase that plays a role in multiple DNA repair events, including double-strand break repair.
• Nonpolar nucleobase analogs illuminate requirements for site-specific DNA cleavage by vaccinia topoisomerase.
• Novel triphosphate phosphohydrolase activity of Clostridium thermocellum TTM, a member of the triphosphate tunnel metalloenzyme superfamily.
• Pulmonary changes due to radiation therapy vs changes due to recurrent neoplasia or infection: use of radiation therapy portal chest radiographs for comparison.
• Reprogramming the tRNA-splicing activity of a bacterial RNA repair enzyme.
• Sonographic diagnosis of neutropenic typhlitis.
• Sonographic spectrum of placental abruption.
• Structural basis for nick recognition by a minimal pluripotent DNA ligase.
• Structure-function analysis of the 3' phosphatase component of T4 polynucleotide kinase/phosphatase.
• Structure-guided mutational analysis of T4 RNA ligase 1.
• Survival of early preimplantation porcine embryos after co-culture with cells producing an avian retrovirus.
• The C-terminal domain of T4 RNA ligase 1 confers specificity for tRNA repair.
• The language of miranda warnings in american jurisdictions: a replication and vocabulary analysis.
• The maltose-maltodextrin transport system of Escherichia coli.
• The pathways and outcomes of mycobacterial NHEJ depend on the structure of the broken DNA ends.
• The poor quality of early evaluations of MR imaging: a reply.
• Vaccinia topoisomerase mutants illuminate roles for Phe59, Gly73, Gln69 and Phe215.
• When faced with a blunt abdominal trauma patient who has hematuria, how should I proceed with the imaging workup?