The crystal structure of pyrimidine/thiamin biosynthesis precursor-like domain-containing protein CAE31940 from proteobacterium Bordetella bronchiseptica RB50, and evolutionary insight into the NMT1/THI5 family

Jacek Bajor; Karolina L. Tkaczuk; Maksymilian Chruszcz; Hutton Chapman; Olga Kagan; Alexei Savchenko; Wladek Minor

doi:10.1007/s10969-014-9180-3

The crystal structure of pyrimidine/thiamin biosynthesis precursor-like domain-containing protein CAE31940 from proteobacterium Bordetella bronchiseptica RB50, and evolutionary insight into the NMT1/THI5 family

Jacek Bajor
, Karolina L. Tkaczuk
, Maksymilian Chruszcz
, Hutton Chapman
, Olga Kagan
, Alexei Savchenko
, Wladek Minor

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

Abstract

We report a 2.0 Å structure of the CAE31940 protein, a proteobacterial NMT1/THI5-like domain-containing protein. We also discuss the primary and tertiary structure similarity with its homologs. The highly conserved FGGXMP motif was identified in CAE31940, which corresponds to the GCCCX motif located in the vicinity of the active center characteristic for THi5-like proteins found in yeast. This suggests that the FGGXMP motif may be a unique hallmark of proteobacterial NMT1/THI5-like proteins.

Original language	English
Pages (from-to)	73-81
Number of pages	9
Journal	Journal of Structural and Functional Genomics
Volume	15
Issue number	2
DOIs	https://doi.org/10.1007/s10969-014-9180-3
State	Published - Jun 2014
Externally published	Yes

Keywords

Bordetella bronchiseptica RB50
Crystal structure
MCSG
NMT1/THI5-like domain-containing protein

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10.1007/s10969-014-9180-3

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Bajor, J., Tkaczuk, K. L., Chruszcz, M., Chapman, H., Kagan, O., Savchenko, A., & Minor, W. (2014). The crystal structure of pyrimidine/thiamin biosynthesis precursor-like domain-containing protein CAE31940 from proteobacterium Bordetella bronchiseptica RB50, and evolutionary insight into the NMT1/THI5 family. Journal of Structural and Functional Genomics, 15(2), 73-81. https://doi.org/10.1007/s10969-014-9180-3

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title = "The crystal structure of pyrimidine/thiamin biosynthesis precursor-like domain-containing protein CAE31940 from proteobacterium Bordetella bronchiseptica RB50, and evolutionary insight into the NMT1/THI5 family",

abstract = "We report a 2.0 {\AA} structure of the CAE31940 protein, a proteobacterial NMT1/THI5-like domain-containing protein. We also discuss the primary and tertiary structure similarity with its homologs. The highly conserved FGGXMP motif was identified in CAE31940, which corresponds to the GCCCX motif located in the vicinity of the active center characteristic for THi5-like proteins found in yeast. This suggests that the FGGXMP motif may be a unique hallmark of proteobacterial NMT1/THI5-like proteins.",

keywords = "Bordetella bronchiseptica RB50, Crystal structure, MCSG, NMT1/THI5-like domain-containing protein",

author = "Jacek Bajor and Tkaczuk, \{Karolina L.\} and Maksymilian Chruszcz and Hutton Chapman and Olga Kagan and Alexei Savchenko and Wladek Minor",

note = "Funding Information: Acknowledgments This research was funded with Federal funds from the National Institute of Health under grants U54-GM074942 and U54-GM094585. The results shown in this report are derived from work performed at Argonne National Laboratory, at the Structural Biology Center of the Advanced Photon Source. Argonne is operated by University of Chicago Argonne, LLC, for the U.S. Department of Energy, Office of Biological and Environmental Research under contract DE-AC02-06CH11357. We thank Dr. Matthew D. Zimmerman for critically reading the manuscript.",

year = "2014",

month = jun,

doi = "10.1007/s10969-014-9180-3",

language = "English",

volume = "15",

pages = "73--81",

journal = "Journal of Structural and Functional Genomics",

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Bajor, J, Tkaczuk, KL, Chruszcz, M, Chapman, H, Kagan, O, Savchenko, A & Minor, W 2014, 'The crystal structure of pyrimidine/thiamin biosynthesis precursor-like domain-containing protein CAE31940 from proteobacterium Bordetella bronchiseptica RB50, and evolutionary insight into the NMT1/THI5 family', Journal of Structural and Functional Genomics, vol. 15, no. 2, pp. 73-81. https://doi.org/10.1007/s10969-014-9180-3

The crystal structure of pyrimidine/thiamin biosynthesis precursor-like domain-containing protein CAE31940 from proteobacterium Bordetella bronchiseptica RB50, and evolutionary insight into the NMT1/THI5 family. / Bajor, Jacek; Tkaczuk, Karolina L.; Chruszcz, Maksymilian et al.
In: Journal of Structural and Functional Genomics, Vol. 15, No. 2, 06.2014, p. 73-81.

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

TY - JOUR

T1 - The crystal structure of pyrimidine/thiamin biosynthesis precursor-like domain-containing protein CAE31940 from proteobacterium Bordetella bronchiseptica RB50, and evolutionary insight into the NMT1/THI5 family

AU - Bajor, Jacek

AU - Tkaczuk, Karolina L.

AU - Chruszcz, Maksymilian

AU - Chapman, Hutton

AU - Kagan, Olga

AU - Savchenko, Alexei

AU - Minor, Wladek

N1 - Funding Information: Acknowledgments This research was funded with Federal funds from the National Institute of Health under grants U54-GM074942 and U54-GM094585. The results shown in this report are derived from work performed at Argonne National Laboratory, at the Structural Biology Center of the Advanced Photon Source. Argonne is operated by University of Chicago Argonne, LLC, for the U.S. Department of Energy, Office of Biological and Environmental Research under contract DE-AC02-06CH11357. We thank Dr. Matthew D. Zimmerman for critically reading the manuscript.

PY - 2014/6

Y1 - 2014/6

N2 - We report a 2.0 Å structure of the CAE31940 protein, a proteobacterial NMT1/THI5-like domain-containing protein. We also discuss the primary and tertiary structure similarity with its homologs. The highly conserved FGGXMP motif was identified in CAE31940, which corresponds to the GCCCX motif located in the vicinity of the active center characteristic for THi5-like proteins found in yeast. This suggests that the FGGXMP motif may be a unique hallmark of proteobacterial NMT1/THI5-like proteins.

AB - We report a 2.0 Å structure of the CAE31940 protein, a proteobacterial NMT1/THI5-like domain-containing protein. We also discuss the primary and tertiary structure similarity with its homologs. The highly conserved FGGXMP motif was identified in CAE31940, which corresponds to the GCCCX motif located in the vicinity of the active center characteristic for THi5-like proteins found in yeast. This suggests that the FGGXMP motif may be a unique hallmark of proteobacterial NMT1/THI5-like proteins.

KW - Bordetella bronchiseptica RB50

KW - Crystal structure

KW - MCSG

KW - NMT1/THI5-like domain-containing protein

UR - https://www.scopus.com/pages/publications/84904063577

U2 - 10.1007/s10969-014-9180-3

DO - 10.1007/s10969-014-9180-3

M3 - Article

C2 - 24908050

AN - SCOPUS:84904063577

SN - 1345-711X

VL - 15

SP - 73

EP - 81

JO - Journal of Structural and Functional Genomics

JF - Journal of Structural and Functional Genomics

IS - 2

ER -

Bajor J, Tkaczuk KL, Chruszcz M, Chapman H, Kagan O, Savchenko A et al. The crystal structure of pyrimidine/thiamin biosynthesis precursor-like domain-containing protein CAE31940 from proteobacterium Bordetella bronchiseptica RB50, and evolutionary insight into the NMT1/THI5 family. Journal of Structural and Functional Genomics. 2014 Jun;15(2):73-81. doi: 10.1007/s10969-014-9180-3