1y0v: Difference between revisions
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'''Crystal structure of anthrax edema factor (EF) in complex with calmodulin and pyrophosphate''' | {{Structure | ||
|PDB= 1y0v |SIZE=350|CAPTION= <scene name='initialview01'>1y0v</scene>, resolution 3.60Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=POP:PYROPHOSPHATE 2-'>POP</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= cya ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1392 Bacillus anthracis]), CALM1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 Xenopus laevis]) | |||
}} | |||
'''Crystal structure of anthrax edema factor (EF) in complex with calmodulin and pyrophosphate''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1Y0V is a [ | 1Y0V is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis] and [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y0V OCA]. | ||
==Reference== | ==Reference== | ||
Calcium-independent calmodulin binding and two-metal-ion catalytic mechanism of anthrax edema factor., Shen Y, Zhukovskaya NL, Guo Q, Florian J, Tang WJ, EMBO J. 2005 Mar 9;24(5):929-41. Epub 2005 Feb 17. PMID:[http:// | Calcium-independent calmodulin binding and two-metal-ion catalytic mechanism of anthrax edema factor., Shen Y, Zhukovskaya NL, Guo Q, Florian J, Tang WJ, EMBO J. 2005 Mar 9;24(5):929-41. Epub 2005 Feb 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15719022 15719022] | ||
[[Category: Adenylate cyclase]] | [[Category: Adenylate cyclase]] | ||
[[Category: Bacillus anthracis]] | [[Category: Bacillus anthracis]] | ||
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[[Category: calmodulin]] | [[Category: calmodulin]] | ||
''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 15:17:01 2008'' | ||
Revision as of 13:17, 20 March 2008
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| 1y0v, resolution 3.60Å | |||||||||||||
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| Ligands: | MG, CA and POP | ||||||||||||
| Gene: | cya (Bacillus anthracis), CALM1 (Xenopus laevis) | ||||||||||||
| Activity: | Adenylate cyclase, with EC number 4.6.1.1 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Crystal structure of anthrax edema factor (EF) in complex with calmodulin and pyrophosphate
Overview
Edema factor (EF), a key anthrax exotoxin, has an anthrax protective antigen-binding domain (PABD) and a calmodulin (CaM)-activated adenylyl cyclase domain. Here, we report the crystal structures of CaM-bound EF, revealing the architecture of EF PABD. CaM has N- and C-terminal domains and each domain can bind two calcium ions. Calcium binding induces the conformational change of CaM from closed to open. Structures of the EF-CaM complex show how EF locks the N-terminal domain of CaM into a closed conformation regardless of its calcium-loading state. This represents a mechanism of how CaM effector alters the calcium affinity of CaM and uncouples the conformational change of CaM from calcium loading. Furthermore, structures of EF-CaM complexed with nucleotides show that EF uses two-metal-ion catalysis, a prevalent mechanism in DNA and RNA polymerases. A histidine (H351) further facilitates the catalysis of EF by activating a water to deprotonate 3'OH of ATP. Mammalian adenylyl cyclases share no structural similarity with EF and they also use two-metal-ion catalysis, suggesting the catalytic mechanism-driven convergent evolution of two structurally diverse adenylyl cyclases.
About this Structure
1Y0V is a Protein complex structure of sequences from Bacillus anthracis and Xenopus laevis. Full crystallographic information is available from OCA.
Reference
Calcium-independent calmodulin binding and two-metal-ion catalytic mechanism of anthrax edema factor., Shen Y, Zhukovskaya NL, Guo Q, Florian J, Tang WJ, EMBO J. 2005 Mar 9;24(5):929-41. Epub 2005 Feb 17. PMID:15719022
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