Crystal Structure of Dephospho-Coenzyme A Kinase from Haemophilus influenzae
Journal of Structural Biology, ISSN: 1047-8477, Vol: 136, Issue: 2, Page: 119-125
2001
- 34Citations
- 26Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations34
- Citation Indexes34
- 34
- CrossRef27
- Captures26
- Readers26
- 26
Article Description
Dephospho-coenzymeA kinase catalyzes the final step in CoA biosynthesis, the phosphorylation of the 3′-hydroxyl group of ribose using ATP as a phosphate donor. The protein from Haemophilus influenzae was cloned and expressed, and its crystal structure was determined at 2.0-Å resolution in complex with ATP. The protein molecule consists of three domains: the canonical nucleotide-binding domain with a five-stranded parallel β-sheet, the substrate-binding α-helical domain, and the lid domain formed by a pair of α-helices. The overall topology of the protein resembles the structures of nucleotide kinases. ATP binds in the P-loop in a manner observed in other kinases. The CoA-binding site is located at the interface of all three domains. The double-pocket structure of the substrate-binding site is unusual for nucleotide kinases. Amino acid residues implicated in substrate binding and catalysis have been identified. The structure analysis suggests large domain movements during the catalytic cycle.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S1047847701944284; http://dx.doi.org/10.1006/jsbi.2001.4428; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0035783037&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/11886213; https://linkinghub.elsevier.com/retrieve/pii/S1047847701944284; https://dx.doi.org/10.1006/jsbi.2001.4428
Elsevier BV
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