Crystal structure of histidine phosphotransfer protein ShpA, an essential regulator of stalk biogenesis in Caulobacter crescentus.
Cell-cycle-regulated stalk biogenesis in Caulobacter crescentus is controlled by a multistep phosphorelay system consisting of the hybrid histidine kinase ShkA, the histidine phosphotransfer (HPt) protein ShpA, and the response regulator TacA. ShpA shuttles phosphoryl groups between ShkA and TacA. When phosphorylated, TacA triggers a downstream transcription cascade for stalk synthesis in an RpoN-dependent manner. The crystal structure of ShpA was determined to 1.52 A resolution. ShpA belongs to a family of monomeric HPt proteins that feature a highly conserved four-helix bundle. The phosphorylatable histidine His56 is located on the surface of the helix bundle and is fully solvent exposed. One end of the four-helix bundle in ShpA is shorter compared with other characterized HPt proteins, whereas the face that potentially interacts with the response regulators is structurally conserved. Similarities of the interaction surface around the phosphorylation site suggest that ShpA is likely to share a common mechanism for molecular recognition and phosphotransfer with yeast phosphotransfer protein YPD1 despite their low overall sequence similarity.
Xu
Qingping
Q
Joint Center for Structural Genomics.
Carlton
Dennis
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Miller
Mitchell D
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Elsliger
Marc-André
MA
Krishna
S Sri
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Abdubek
Polat
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Astakhova
Tamara
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Burra
Prasad
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Chiu
Hsiu-Ju
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Clayton
Thomas
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Deller
Marc C
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Duan
Lian
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Elias
Ylva
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Feuerhelm
Julie
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Grant
Joanna C
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Grzechnik
Anna
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Grzechnik
Slawomir K
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Han
Gye Won
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Jaroszewski
Lukasz
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Jin
Kevin K
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Klock
Heath E
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Knuth
Mark W
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Kozbial
Piotr
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Kumar
Abhinav
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Marciano
David
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McMullan
Daniel
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Morse
Andrew T
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Nigoghossian
Edward
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Okach
Linda
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Oommachen
Silvya
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Paulsen
Jessica
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Reyes
Ron
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Rife
Christopher L
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Sefcovic
Natasha
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Trame
Christine
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Trout
Christina V
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van den Bedem
Henry
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Weekes
Dana
D
Hodgson
Keith O
KO
Wooley
John
J
Deacon
Ashley M
AM
Godzik
Adam
A
Lesley
Scott A
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Wilson
Ian A
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D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D016935:Caulobacter crescentus / Q000378:metabolism*; D018360:Crystallography, X-Ray; D006639:Histidine / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010766:Phosphorylation; D010770:Phosphotransferases / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation
D001426:Bacterial Proteins; D006639:Histidine; D010770:Phosphotransferases