| Item type: | Article | ||||||||||||||||||||||||||||||||||||
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| Journal or Publication Title: | Journal of molecular biology | ||||||||||||||||||||||||||||||||||||
| Publisher: | ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD | ||||||||||||||||||||||||||||||||||||
| Place of Publication: | LONDON | ||||||||||||||||||||||||||||||||||||
| Volume: | 338 | ||||||||||||||||||||||||||||||||||||
| Number of Issue or Book Chapter: | 2 | ||||||||||||||||||||||||||||||||||||
| Page Range: | pp. 287-297 | ||||||||||||||||||||||||||||||||||||
| Date: | 2004 | ||||||||||||||||||||||||||||||||||||
| Institutions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie | ||||||||||||||||||||||||||||||||||||
| Identification Number: |
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| Classification: |
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| Keywords: | CHEMOTAXIS SIGNAL-TRANSDUCTION; PROTEIN SECONDARY STRUCTURE; CHEMICAL-SHIFT INDEX; FIXJ RECEIVER DOMAIN; BACTERIAL CHEMOTAXIS; RHIZOBIUM-MELILOTI; SINORHIZOBIUM-MELILOTI; NMR-SPECTROSCOPY; ESCHERICHIA-COLI; ACTIVATED CHEY; chemotaxis; domain interaction; NMR structure; response regulator; retro-phosphorylation | ||||||||||||||||||||||||||||||||||||
| Dewey Decimal Classification: | 500 Science > 570 Life sciences | ||||||||||||||||||||||||||||||||||||
| Status: | Published | ||||||||||||||||||||||||||||||||||||
| Refereed: | Unknown | ||||||||||||||||||||||||||||||||||||
| Created at the University of Regensburg: | Unknown | ||||||||||||||||||||||||||||||||||||
| Item ID: | 16606 |
Web of ScienceAbstract
The chemotactic signalling chain to the flagellar motor of Sinorhizobium meliloti features a new type of response regulator, CheY2. CheY2 activated by phosphorylation (CheY2-P) controls the rotary speed of the flagellar motor (instead of reversing the sense of rotation), and it is efficiently dephosphorylated by phospho-retrotransfer to the cognate kinase, CheA. Here, we report the NMR solution ...
Abstract
The chemotactic signalling chain to the flagellar motor of Sinorhizobium meliloti features a new type of response regulator, CheY2. CheY2 activated by phosphorylation (CheY2-P) controls the rotary speed of the flagellar motor (instead of reversing the sense of rotation), and it is efficiently dephosphorylated by phospho-retrotransfer to the cognate kinase, CheA. Here, we report the NMR solution structures of the Mg2+-complex of inactive CheY2, and of activated CheY2-BeF3, a stable analogue of CheY2-P, to an overall root mean square deviation of 0.042 nm and 0.027 nm, respectively. The 14 kDa. CheY2 protein exhibits a characteristic open (alpha/beta)(5) conformation. Modification of CheY2 by BeF3- leads to large conformational changes of the protein, which are in the limits of error identical with those observed by phosphorylation of the active-centre residue Asp58. In BeF3-activated CheY2, the position of Thr88-OH favours the formation of a hydrogen bond with the active site, Asp58-BeF3, similar to BeF3-activated CheY from Escherichia coli. In contrast to E. coli, this reorientation is not involved in a Tyr-Thr-coupling mechanism, that propagates the signal from the incoming phosphoryl group to the C-terminally located FliM-binding surface. Rather, a rearrangement of the Phe59 side-chain to interact with Ile86-Leu95-Val96 along with a displacement of alpha4 towards beta5 is stabilised in S. meliloti. The resulting, activation-induced, compact alpha4-beta5-alpha5 surface forms a unique binding domain suited for specific interaction with and signalling to a rotary motor that requires a gradual speed control. We propose that these new features of response regulator activation, compared to other two-component systems, are the key for the observed unique phosphorylation, dephosphorylation and motor control mechanisms in S. meliloti. (C) 2004 Elsevier Ltd. All rights reserved.
Metadata last modified: 29 Sep 2021 07:38
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