Pentapeptide repeat proteins

Matthew W. Vetting; Subray S. Hegde; J. Eduardo Fajardo; Andras Fiser; Steven L. Roderick; Howard E. Takiff; John S. Blanchard

doi:10.1021/bi052130w

Pentapeptide repeat proteins

Matthew W. Vetting, Subray S. Hegde, J. Eduardo Fajardo, Andras Fiser, Steven L. Roderick, Howard E. Takiff, John S. Blanchard

Research output: Contribution to journal › Review article › peer-review

139 Scopus citations

Abstract

The pentapeptide repeat protein (PRP) family has more than 500 members in the prokaryotic and eukaryotic kingdoms. These proteins are composed of, or contain domains composed of, tandemly repeated amino acid sequences with a consensus sequence of [S,T,A,V][D,N][L,F][S,T,R][G]. The biochemical function of the vast majority of PRP family members is unknown. The three-dimensional structure of the first member of the PRP family was determined for the fluoroquinolone resistance protein (MfpA) from Mycobacterium tuberculosis. The structure revealed that the pentapeptide repeats encode the folding of a novel right-handed quadrilateral β-helix. MfpA binds to DNA gyrase and inhibits its activity. The rod-shaped, dimeric protein exhibits remarkable similarity in size, shape, and electrostatics to DNA.

Original language	English (US)
Pages (from-to)	1-10
Number of pages	10
Journal	Biochemistry
Volume	45
Issue number	1
DOIs	https://doi.org/10.1021/bi052130w
State	Published - Jan 10 2006

ASJC Scopus subject areas

Biochemistry

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1021/bi052130w

Cite this

@article{f80b9da8af35407d96712c30b8c748ec,

title = "Pentapeptide repeat proteins",

abstract = "The pentapeptide repeat protein (PRP) family has more than 500 members in the prokaryotic and eukaryotic kingdoms. These proteins are composed of, or contain domains composed of, tandemly repeated amino acid sequences with a consensus sequence of [S,T,A,V][D,N][L,F][S,T,R][G]. The biochemical function of the vast majority of PRP family members is unknown. The three-dimensional structure of the first member of the PRP family was determined for the fluoroquinolone resistance protein (MfpA) from Mycobacterium tuberculosis. The structure revealed that the pentapeptide repeats encode the folding of a novel right-handed quadrilateral β-helix. MfpA binds to DNA gyrase and inhibits its activity. The rod-shaped, dimeric protein exhibits remarkable similarity in size, shape, and electrostatics to DNA.",

author = "Vetting, {Matthew W.} and Hegde, {Subray S.} and Fajardo, {J. Eduardo} and Andras Fiser and Roderick, {Steven L.} and Takiff, {Howard E.} and Blanchard, {John S.}",

year = "2006",

month = jan,

day = "10",

doi = "10.1021/bi052130w",

language = "English (US)",

volume = "45",

pages = "1--10",

journal = "Biochemistry",

issn = "0006-2960",

publisher = "American Chemical Society",

number = "1",

}

TY - JOUR

T1 - Pentapeptide repeat proteins

AU - Vetting, Matthew W.

AU - Hegde, Subray S.

AU - Fajardo, J. Eduardo

AU - Fiser, Andras

AU - Roderick, Steven L.

AU - Takiff, Howard E.

AU - Blanchard, John S.

PY - 2006/1/10

Y1 - 2006/1/10

N2 - The pentapeptide repeat protein (PRP) family has more than 500 members in the prokaryotic and eukaryotic kingdoms. These proteins are composed of, or contain domains composed of, tandemly repeated amino acid sequences with a consensus sequence of [S,T,A,V][D,N][L,F][S,T,R][G]. The biochemical function of the vast majority of PRP family members is unknown. The three-dimensional structure of the first member of the PRP family was determined for the fluoroquinolone resistance protein (MfpA) from Mycobacterium tuberculosis. The structure revealed that the pentapeptide repeats encode the folding of a novel right-handed quadrilateral β-helix. MfpA binds to DNA gyrase and inhibits its activity. The rod-shaped, dimeric protein exhibits remarkable similarity in size, shape, and electrostatics to DNA.

AB - The pentapeptide repeat protein (PRP) family has more than 500 members in the prokaryotic and eukaryotic kingdoms. These proteins are composed of, or contain domains composed of, tandemly repeated amino acid sequences with a consensus sequence of [S,T,A,V][D,N][L,F][S,T,R][G]. The biochemical function of the vast majority of PRP family members is unknown. The three-dimensional structure of the first member of the PRP family was determined for the fluoroquinolone resistance protein (MfpA) from Mycobacterium tuberculosis. The structure revealed that the pentapeptide repeats encode the folding of a novel right-handed quadrilateral β-helix. MfpA binds to DNA gyrase and inhibits its activity. The rod-shaped, dimeric protein exhibits remarkable similarity in size, shape, and electrostatics to DNA.

UR - http://www.scopus.com/inward/record.url?scp=30144433013&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=30144433013&partnerID=8YFLogxK

U2 - 10.1021/bi052130w

DO - 10.1021/bi052130w

M3 - Review article

C2 - 16388575

AN - SCOPUS:30144433013

SN - 0006-2960

VL - 45

SP - 1

EP - 10

JO - Biochemistry

JF - Biochemistry

IS - 1

ER -

Pentapeptide repeat proteins

Abstract

ASJC Scopus subject areas

UN SDGs

Access to Document

Other files and links

Fingerprint

Cite this