Evidence map›Paper›PMID 19380375›Full record

ArticleNucleic acids research2009

Crystal structure of the beta beta alpha-Me type II restriction endonuclease Hpy99I with target DNA.

Monika Sokolowska, Honorata Czapinska, Matthias Bochtler

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Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

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0cells of the map it votes in
41citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

Who cites it

41 citing papers in PubMed.

  1. Article
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  13. Activity and structure of EcoKMcrA.Nucleic acids research · 2018
    Article
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  15. Article
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  18. Review
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4 · The record

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5 · Who and what money

Authors and funding

3 authors.

Monika SokolowskaInternational Institute of Molecular and Cell Biology, Trojdena 4, 02-109 Warsaw, Poland.
Honorata Czapinska
Matthias Bochtler

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The beta beta alpha-Me restriction endonuclease (REase) Hpy99I recognizes the CGWCG target sequence and cleaves it with unusual stagger (five nucleotide 5'-recessed ends). Here we present the crystal structure of the specific complex of the dimeric enzyme with DNA. The Hpy99I protomer consists of an antiparallel beta-barrel and two beta 4 alpha 2 repeats. Each repeat coordinates a structural zinc ion with four cysteine thiolates in two CXXC motifs. The beta beta alpha-Me region of the second beta 4 alpha 2 repeat holds the catalytic metal ion (or its sodium surrogate) via Asp148 and Asn165 and activates a water molecule with the general base His149. In the specific complex, Hpy99I forms a ring-like structure around the DNA that contacts DNA bases on the major and minor groove sides via the first and second beta 4 alpha 2 repeats, respectively. Hpy99I interacts with the central base pair of the recognition sequence only on the minor groove side, where A:T resembles T:A and G:C is similar to C:G. The Hpy99I-DNA co-crystal structure provides the first detailed illustration of the beta beta alpha-Me site in REases and complements structural information on the use of this active site motif in other groups of endonucleases such as homing endonucleases (e.g. I-PpoI) and Holliday junction resolvases (e.g. T4 endonuclease VII).

Indexed as

Amino Acid SequenceCatalytic DomainCrystallography, X-RayDeoxyribonucleases, Type II Site-SpecificDNAMetalsModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedProtein MultimerizationProtein SubunitsDeoxyribonucleases, Type II Site-SpecificDNAMetalsProtein Subunits

Identifiers

PMID19380375
PMCPMC2699513

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.