1y0v

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[[Image:1y0v.gif|left|200px]]<br /><applet load="1y0v" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1y0v.gif|left|200px]]
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caption="1y0v, resolution 3.60&Aring;" />
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'''Crystal structure of anthrax edema factor (EF) in complex with calmodulin and pyrophosphate'''<br />
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{{Structure
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|PDB= 1y0v |SIZE=350|CAPTION= <scene name='initialview01'>1y0v</scene>, resolution 3.60&Aring;
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|SITE=
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|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>
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|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]
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|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])
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}}
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'''Crystal structure of anthrax edema factor (EF) in complex with calmodulin and pyrophosphate'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1Y0V is a [http://en.wikipedia.org/wiki/Protein_complex 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] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=POP:'>POP</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=1Y0V OCA].
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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==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15719022 15719022]
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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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:00:39 2008''
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''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


PDB ID 1y0v

Drag the structure with the mouse to rotate
, resolution 3.60Å
Ligands: , and
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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