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1y10

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{{STRUCTURE_1y10| PDB=1y10 | SCENE= }}
{{STRUCTURE_1y10| PDB=1y10 | SCENE= }}
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'''Mycobacterial adenylyl cyclase Rv1264, holoenzyme, inhibited state'''
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===Mycobacterial adenylyl cyclase Rv1264, holoenzyme, inhibited state===
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==Overview==
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Class III adenylyl cyclases contain catalytic and regulatory domains, yet structural insight into their interactions is missing. We show that the mycobacterial adenylyl cyclase Rv1264 is rendered a pH sensor by its N-terminal domain. In the structure of the inhibited state, catalytic and regulatory domains share a large interface involving catalytic residues. In the structure of the active state, the two catalytic domains rotate by 55 degrees to form two catalytic sites at their interface. Two alpha helices serve as molecular switches. Mutagenesis is consistent with a regulatory role of the structural transition, and we suggest that the transition is regulated by pH.
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{{ABSTRACT_PUBMED_15890882}}
==About this Structure==
==About this Structure==
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[[Category: Tews, I.]]
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[[Category: Adenylyl cyclase fold]]
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Revision as of 00:05, 29 July 2008

Image:1y10.png

Template:STRUCTURE 1y10

Mycobacterial adenylyl cyclase Rv1264, holoenzyme, inhibited state

Template:ABSTRACT PUBMED 15890882

About this Structure

1Y10 is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

The structure of a pH-sensing mycobacterial adenylyl cyclase holoenzyme., Tews I, Findeisen F, Sinning I, Schultz A, Schultz JE, Linder JU, Science. 2005 May 13;308(5724):1020-3. PMID:15890882

Page seeded by OCA on Tue Jul 29 03:05:14 2008

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