Structure of microcin J25, a peptide inhibitor of bacterial RNA polymerase, is a lassoed tail

Kelly Anne Wilson; Markus Kalkum; Jennifer Ottesen; Julia Yuzenkova; Brian T. Chait; Robert Landick; Tom Muir; Konstantin Severinov; Seth A. Darst

doi:10.1021/ja036756q

Structure of microcin J25, a peptide inhibitor of bacterial RNA polymerase, is a lassoed tail

Kelly Anne Wilson, Markus Kalkum, Jennifer Ottesen, Julia Yuzenkova, Brian T. Chait, Robert Landick, Tom Muir, Konstantin Severinov, Seth A. Darst

Research output: Contribution to journal › Article › peer-review

214 Scopus citations

Abstract

Microcin J25 (MccJ25) is a 21-amino acid peptide inhibitor active against the DNA-dependent RNA polymerase of Gram negative bacteria. Previously, the structure of MccJ25 was reported to be a head-to-tail circle, cyclo(-G ¹GAGHVPEYF¹⁰VGIGTPISFY²⁰G-). On the basis of biochemical studies, mass spectrometry, and NMR, we show that this structure is incorrect, and that the peptide has an extraordinary structural fold. MccJ25 contains an internal lactam linkage between the α-amino group of Glyl and the γ-carboxyl of Glu8. The tail (Tyr9-Gly21) passes through the ring (Gly1-Glu8), with Phe19 and Tyr20 straddling each side of the ring, sterically trapping the tail in a noncovalent interaction we call a lassoed tail.

Original language	English (US)
Pages (from-to)	12475-12483
Number of pages	9
Journal	Journal of the American Chemical Society
Volume	125
Issue number	41
DOIs	https://doi.org/10.1021/ja036756q
State	Published - Oct 15 2003
Externally published	Yes

All Science Journal Classification (ASJC) codes

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

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10.1021/ja036756q

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title = "Structure of microcin J25, a peptide inhibitor of bacterial RNA polymerase, is a lassoed tail",

abstract = "Microcin J25 (MccJ25) is a 21-amino acid peptide inhibitor active against the DNA-dependent RNA polymerase of Gram negative bacteria. Previously, the structure of MccJ25 was reported to be a head-to-tail circle, cyclo(-G 1GAGHVPEYF10VGIGTPISFY20G-). On the basis of biochemical studies, mass spectrometry, and NMR, we show that this structure is incorrect, and that the peptide has an extraordinary structural fold. MccJ25 contains an internal lactam linkage between the α-amino group of Glyl and the γ-carboxyl of Glu8. The tail (Tyr9-Gly21) passes through the ring (Gly1-Glu8), with Phe19 and Tyr20 straddling each side of the ring, sterically trapping the tail in a noncovalent interaction we call a lassoed tail.",

author = "Wilson, {Kelly Anne} and Markus Kalkum and Jennifer Ottesen and Julia Yuzenkova and Chait, {Brian T.} and Robert Landick and Tom Muir and Konstantin Severinov and Darst, {Seth A.}",

year = "2003",

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doi = "10.1021/ja036756q",

language = "English (US)",

volume = "125",

pages = "12475--12483",

journal = "Journal of the American Chemical Society",

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TY - JOUR

T1 - Structure of microcin J25, a peptide inhibitor of bacterial RNA polymerase, is a lassoed tail

AU - Wilson, Kelly Anne

AU - Kalkum, Markus

AU - Ottesen, Jennifer

AU - Yuzenkova, Julia

AU - Chait, Brian T.

AU - Landick, Robert

AU - Muir, Tom

AU - Severinov, Konstantin

AU - Darst, Seth A.

PY - 2003/10/15

Y1 - 2003/10/15

N2 - Microcin J25 (MccJ25) is a 21-amino acid peptide inhibitor active against the DNA-dependent RNA polymerase of Gram negative bacteria. Previously, the structure of MccJ25 was reported to be a head-to-tail circle, cyclo(-G 1GAGHVPEYF10VGIGTPISFY20G-). On the basis of biochemical studies, mass spectrometry, and NMR, we show that this structure is incorrect, and that the peptide has an extraordinary structural fold. MccJ25 contains an internal lactam linkage between the α-amino group of Glyl and the γ-carboxyl of Glu8. The tail (Tyr9-Gly21) passes through the ring (Gly1-Glu8), with Phe19 and Tyr20 straddling each side of the ring, sterically trapping the tail in a noncovalent interaction we call a lassoed tail.

AB - Microcin J25 (MccJ25) is a 21-amino acid peptide inhibitor active against the DNA-dependent RNA polymerase of Gram negative bacteria. Previously, the structure of MccJ25 was reported to be a head-to-tail circle, cyclo(-G 1GAGHVPEYF10VGIGTPISFY20G-). On the basis of biochemical studies, mass spectrometry, and NMR, we show that this structure is incorrect, and that the peptide has an extraordinary structural fold. MccJ25 contains an internal lactam linkage between the α-amino group of Glyl and the γ-carboxyl of Glu8. The tail (Tyr9-Gly21) passes through the ring (Gly1-Glu8), with Phe19 and Tyr20 straddling each side of the ring, sterically trapping the tail in a noncovalent interaction we call a lassoed tail.

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U2 - 10.1021/ja036756q

DO - 10.1021/ja036756q

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AN - SCOPUS:0141919821

SN - 0002-7863

VL - 125

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JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 41

ER -

Structure of microcin J25, a peptide inhibitor of bacterial RNA polymerase, is a lassoed tail

Abstract

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