Inhibition of chlamydial class Ic ribonucleotide reductase by C-terminal peptides from protein R2

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Fältnamn	Indikatorer	Metadata
000		03671naa a2200445 4500
001		oai:DiVA.org:su-70146
003		SwePub
008		120117s2011 \| \|\|\|\|\|\|\|\|\|\|\|000 \|\|eng\|
024	7	a https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-701462 URI
024	7	a https://doi.org/10.1002/psc.13992 DOI
040		a (SwePub)su
041		a engb eng
042		9 SwePub
072	7	a ref2 swepub-contenttype
072	7	a art2 swepub-publicationtype
100	1	a Öhrström, Mariau Stockholms universitet,Institutionen för biokemi och biofysik4 aut
245	1 0	a Inhibition of chlamydial class Ic ribonucleotide reductase by C-terminal peptides from protein R2
264		c 2011-10-04
264	1	b Wiley,c 2011
338		a print2 rdacarrier
500		a authorCount>6
520		a Chlamydia trachomatis ribonucleotide reductase (RNR) is a class Ic RNR. It has two homodimeric subunits: proteins R1 and R2. Class Ic protein R2 in its most active form has a manganese-iron metal cofactor, which functions in catalysis like the tyrosyl radical in classical class Ia and Ib RNRs. Oligopeptides with the same sequence as the C-terminus of C. trachomatis protein R2 inhibit the catalytic activity of C. trachomatis RNR, showing that the class Ic enzyme shares a similar highly specific inhibition mechanism with the previously studied radical-containing class Ia and Ib RNRs. The results indicate that the catalytic mechanism of this class of RNRs with a manganese-iron cofactor is similar to that of the tyrosyl-radical-containing RNRs, involving reversible long-range radical transfer between proteins R1 and R2. The competitive binding of the inhibitory R2-derived oligopeptide blocks the transfer pathway. We have constructed three-dimensional structure models of C. trachomatis protein R1, based on homologous R1 crystal structures, and used them to discuss possible binding modes of the peptide to protein R1. Typical half maximal inhibitory concentration values for C. trachomatis RNR are about 200 µ m for a 20-mer peptide, indicating a less efficient inhibition compared with those for an equally long peptide in the Escherichia coli class Ia RNR. A possible explanation is that the C. trachomatis R1/R2 complex has other important interactions, in addition to the binding mediated by the R1 interaction with the C-terminus of protein R2.
650	7	a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe
650	7	a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng
653		a class Ic ribonucleotide reductase
653		a manganese–iron cofactor
653		a subunit interaction inhibitor
653		a protein R2 C-terminus
653		a oligopeptide inhibitor
653		a Biophysics
653		a biofysik
700	1	a Popović-Bijelić, Ana,d 1976-u Stockholms universitet,Institutionen för biokemi och biofysik4 aut0 (Swepub:su)anpo6406
700	1	a Luo, Jinghui4 aut
700	1	a Stenmark, Pålu Stockholms universitet,Institutionen för biokemi och biofysik4 aut0 (Swepub:su)stenm
700	1	a Högbom, Martinu Stockholms universitet,Institutionen för biokemi och biofysik4 aut0 (Swepub:su)hogbom
700	1	a Gräslund, Astridu Stockholms universitet,Institutionen för biokemi och biofysik4 aut0 (Swepub:su)astrid
710	2	a Stockholms universitetb Institutionen för biokemi och biofysik4 org
773	0	t Journal of Peptide Scienced : Wileyg 17:11, s. 756-762q 17:11<756-762x 1075-2617x 1099-1387
856	4 8	u https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-70146
856	4 8	u https://doi.org/10.1002/psc.1399

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Av författaren/redakt...: Öhrström, Maria; Popović-Bijelić, ...; Luo, Jinghui; Stenmark, Pål; Högbom, Martin; Gräslund, Astrid

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