1y10
From Proteopedia
(New page: 200px<br /><applet load="1y10" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y10, resolution 2.30Å" /> '''Mycobacterial adenyl...) |
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| - | [[Image:1y10.gif|left|200px]]<br /><applet load="1y10" size=" | + | [[Image:1y10.gif|left|200px]]<br /><applet load="1y10" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1y10, resolution 2.30Å" /> | caption="1y10, resolution 2.30Å" /> | ||
'''Mycobacterial adenylyl cyclase Rv1264, holoenzyme, inhibited state'''<br /> | '''Mycobacterial adenylyl cyclase Rv1264, holoenzyme, inhibited state'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Class III adenylyl cyclases contain catalytic and regulatory domains, yet | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1Y10 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with CA and 1PE as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Adenylate_cyclase Adenylate cyclase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.6.1.1 4.6.1.1] Full crystallographic information is available from [http:// | + | 1Y10 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=1PE:'>1PE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Adenylate_cyclase Adenylate cyclase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.6.1.1 4.6.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y10 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Findeisen, F.]] | [[Category: Findeisen, F.]] | ||
| - | [[Category: Linder, J | + | [[Category: Linder, J U.]] |
[[Category: Schultz, A.]] | [[Category: Schultz, A.]] | ||
| - | [[Category: Schultz, J | + | [[Category: Schultz, J E.]] |
[[Category: Sinning, I.]] | [[Category: Sinning, I.]] | ||
[[Category: Tews, I.]] | [[Category: Tews, I.]] | ||
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[[Category: adenylyl cyclase fold]] | [[Category: adenylyl cyclase fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:00:43 2008'' |
Revision as of 14:00, 21 February 2008
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Mycobacterial adenylyl cyclase Rv1264, holoenzyme, inhibited state
Overview
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.
About this Structure
1Y10 is a Single protein structure of sequence from Mycobacterium tuberculosis with and as ligands. Active as Adenylate cyclase, with EC number 4.6.1.1 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
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