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Bicarbonate activation of adenylyl cyclase via promotion of catalytic active site closure and metal recruitment.

Title data

Steegborn, Clemens ; Litvin, Tatiana N. ; Levin, Lonny R. ; Buck, Jochen ; Wu, Hao:
Bicarbonate activation of adenylyl cyclase via promotion of catalytic active site closure and metal recruitment.
In: Nature Structural & Molecular Biology. Vol. 12 (January 2005) Issue 1 . - pp. 32-37.
ISSN 1545-9985
DOI: https://doi.org/10.1038/nsmb880

Abstract in another language

In an evolutionarily conserved signaling pathway, 'soluble' adenylyl cyclases (sACs) synthesize the ubiquitous second messenger cyclic adenosine 3',5'-monophosphate (cAMP) in response to bicarbonate and calcium signals. Here, we present crystal structures of a cyanobacterial sAC enzyme in complex with ATP analogs, calcium and bicarbonate, which represent distinct catalytic states of the enzyme. The structures reveal that calcium occupies the first ion-binding site and directly mediates nucleotide binding. The single ion-occupied, nucleotide-bound state defines a novel, open adenylyl cyclase state. In contrast, bicarbonate increases the catalytic rate by inducing marked active site closure and recruiting a second, catalytic ion. The phosphates of the bound substrate analogs are rearranged, which would facilitate product formation and release. The mechanisms of calcium and bicarbonate sensing define a reaction pathway involving active site closure and metal recruitment that may be universal for class III cyclases.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 15689969
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry > Chair Biochemistry - Univ.-Prof. Dr. Clemens Steegborn
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry
Result of work at the UBT: No
DDC Subjects: 500 Science > 540 Chemistry
Date Deposited: 14 Apr 2015 10:11
Last Modified: 14 Apr 2015 10:11
URI: https://eref.uni-bayreuth.de/id/eprint/10136