1ybt

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[[Image:1ybt.gif|left|200px]]
[[Image:1ybt.gif|left|200px]]
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{{Structure
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|PDB= 1ybt |SIZE=350|CAPTION= <scene name='initialview01'>1ybt</scene>, resolution 2.31&Aring;
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The line below this paragraph, containing "STRUCTURE_1ybt", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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|GENE= Rv1900c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83331 Mycobacterium tuberculosis CDC1551])
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|DOMAIN=
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{{STRUCTURE_1ybt| PDB=1ybt | SCENE= }}
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|RELATEDENTRY=[[1ybu|1YBU]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ybt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ybt OCA], [http://www.ebi.ac.uk/pdbsum/1ybt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ybt RCSB]</span>
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}}
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'''MYCOBACTERIUM TUBERCULOSIS ADENYLYL CYCLASE, RV1900C CHD'''
'''MYCOBACTERIUM TUBERCULOSIS ADENYLYL CYCLASE, RV1900C CHD'''
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[[Category: Sprang, S R.]]
[[Category: Sprang, S R.]]
[[Category: Wetterer, M.]]
[[Category: Wetterer, M.]]
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[[Category: chd]]
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[[Category: Chd]]
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[[Category: cyclase homology domain]]
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[[Category: Cyclase homology domain]]
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[[Category: rv1900c]]
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[[Category: Rv1900c]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:07:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:02:08 2008''
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Revision as of 13:07, 3 May 2008

Image:1ybt.gif

Template:STRUCTURE 1ybt

MYCOBACTERIUM TUBERCULOSIS ADENYLYL CYCLASE, RV1900C CHD


Overview

Rv1900c, a Mycobacterium tuberculosis adenylyl cyclase, is composed of an N-terminal alpha/beta-hydrolase domain and a C-terminal cyclase homology domain. It has an unusual 7% guanylyl cyclase side-activity. A canonical substrate-defining lysine and a catalytic asparagine indispensable for mammalian adenylyl cyclase activity correspond to N342 and H402 in Rv1900c. Mutagenic analysis indicates that these residues are dispensable for activity of Rv1900c. Structures of the cyclase homology domain, solved to 2.4 A both with and without an ATP analog, form isologous, but asymmetric homodimers. The noncanonical N342 and H402 do not interact with the substrate. Subunits of the unliganded open dimer move substantially upon binding substrate, forming a closed dimer similar to the mammalian cyclase heterodimers, in which one interfacial active site is occupied and the quasi-dyad-related active site is occluded. This asymmetry indicates that both active sites cannot simultaneously be catalytically active. Such a mechanism of half-of-sites-reactivity suggests that mammalian heterodimeric adenylyl cyclases may have evolved from gene duplication of a primitive prokaryote-type cyclase, followed by loss of function in one active site.

About this Structure

1YBT is a Single protein structure of sequence from Mycobacterium tuberculosis cdc1551. Full crystallographic information is available from OCA.

Reference

Origin of asymmetry in adenylyl cyclases: structures of Mycobacterium tuberculosis Rv1900c., Sinha SC, Wetterer M, Sprang SR, Schultz JE, Linder JU, EMBO J. 2005 Feb 23;24(4):663-73. Epub 2005 Jan 27. PMID:15678099 Page seeded by OCA on Sat May 3 16:07:25 2008

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