1ybu
From Proteopedia
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| - | [[Image:1ybu.gif|left|200px]] | + | [[Image:1ybu.gif|left|200px]] |
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| - | '''Mycobacterium tuberculosis adenylyl cyclase Rv1900c CHD, in complex with a substrate analog.''' | + | {{Structure |
| + | |PDB= 1ybu |SIZE=350|CAPTION= <scene name='initialview01'>1ybu</scene>, resolution 2.40Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER'>APC</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= Rv1900c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 Mycobacterium tuberculosis H37Rv]) | ||
| + | }} | ||
| + | |||
| + | '''Mycobacterium tuberculosis adenylyl cyclase Rv1900c CHD, in complex with a substrate analog.''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1YBU is a [ | + | 1YBU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_h37rv Mycobacterium tuberculosis h37rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YBU OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15678099 15678099] |
[[Category: Adenylate cyclase]] | [[Category: Adenylate cyclase]] | ||
[[Category: Mycobacterium tuberculosis h37rv]] | [[Category: Mycobacterium tuberculosis h37rv]] | ||
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[[Category: rv1900c]] | [[Category: rv1900c]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:20:52 2008'' |
Revision as of 13:20, 20 March 2008
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| , resolution 2.40Å | |||||||
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| Ligands: | and | ||||||
| Gene: | Rv1900c (Mycobacterium tuberculosis H37Rv) | ||||||
| Activity: | Adenylate cyclase, with EC number 4.6.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Mycobacterium tuberculosis adenylyl cyclase Rv1900c CHD, in complex with a substrate analog.
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
1YBU is a Single protein structure of sequence from Mycobacterium tuberculosis h37rv. 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
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