1yk9: Difference between revisions
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'''Crystal structure of a mutant form of the mycobacterial adenylyl cyclase Rv1625c''' | '''Crystal structure of a mutant form of the mycobacterial adenylyl cyclase Rv1625c''' | ||
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[[Category: TBSGC, TB Structural Genomics Consortium.]] | [[Category: TBSGC, TB Structural Genomics Consortium.]] | ||
[[Category: Visweswariah, S S.]] | [[Category: Visweswariah, S S.]] | ||
[[Category: | [[Category: Beta-alpha-beta sandwich]] | ||
[[Category: | [[Category: Protein structure initiative]] | ||
[[Category: | [[Category: Psi]] | ||
[[Category: | [[Category: Structural genomic]] | ||
[[Category: | [[Category: Tb structural genomics consortium]] | ||
[[Category: | [[Category: Tbsgc]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:25:36 2008'' | |||
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Revision as of 16:25, 3 May 2008
Crystal structure of a mutant form of the mycobacterial adenylyl cyclase Rv1625c
OverviewOverview
The Rv1625c Class III adenylyl cyclase from Mycobacterium tuberculosis is a homodimeric enzyme with two catalytic centers at the dimer interface, and shows sequence similarity with the mammalian adenylyl and guanylyl cyclases. Mutation of the substrate-specifying residues in the catalytic domain of Rv1625c, either independently or together, to those present in guanylyl cyclases not only failed to confer guanylyl cyclase activity to the protein, but also severely abrogated the adenylyl cyclase activity of the enzyme. Biochemical analysis revealed alterations in the behavior of the mutants on ion-exchange chromatography, indicating differences in the surface-exposed charge upon mutation of substrate-specifying residues. The mutant proteins showed alterations in oligomeric status as compared to the wild-type enzyme, and differing abilities to heterodimerize with the wild-type protein. The crystal structure of a mutant has been solved to a resolution of 2.7A. On the basis of the structure, and additional biochemical studies, we provide possible reasons for the altered properties of the mutant proteins, as well as highlight unique structural features of the Rv1625c adenylyl cyclase.
About this StructureAbout this Structure
1YK9 is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
ReferenceReference
A structural basis for the role of nucleotide specifying residues in regulating the oligomerization of the Rv1625c adenylyl cyclase from M. tuberculosis., Ketkar AD, Shenoy AR, Ramagopal UA, Visweswariah SS, Suguna K, J Mol Biol. 2006 Mar 3;356(4):904-16. Epub 2005 Dec 22. PMID:16403515 Page seeded by OCA on Sat May 3 16:25:36 2008
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- Adenylate cyclase
- Mycobacterium tuberculosis
- Single protein
- Ketkar, A D.
- Ramagopal, U A.
- Shenoy, A R.
- Suguna, K.
- TBSGC, TB Structural Genomics Consortium.
- Visweswariah, S S.
- Beta-alpha-beta sandwich
- Protein structure initiative
- Psi
- Structural genomic
- Tb structural genomics consortium
- Tbsgc