2fjt
From Proteopedia
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| - | [[Image:2fjt.gif|left|200px]] | + | [[Image:2fjt.gif|left|200px]] |
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| - | '''Adenylyl cyclase class iv from Yersinia pestis''' | + | {{Structure |
| + | |PDB= 2fjt |SIZE=350|CAPTION= <scene name='initialview01'>2fjt</scene>, resolution 1.901Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</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= | ||
| + | }} | ||
| + | |||
| + | '''Adenylyl cyclase class iv from Yersinia pestis''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2FJT is a [ | + | 2FJT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FJT OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of the class IV adenylyl cyclase reveals a novel fold., Gallagher DT, Smith NN, Kim SK, Heroux A, Robinson H, Reddy PT, J Mol Biol. 2006 Sep 8;362(1):114-22. Epub 2006 Aug 14. PMID:[http:// | + | Structure of the class IV adenylyl cyclase reveals a novel fold., Gallagher DT, Smith NN, Kim SK, Heroux A, Robinson H, Reddy PT, J Mol Biol. 2006 Sep 8;362(1):114-22. Epub 2006 Aug 14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16905149 16905149] |
[[Category: Adenylate cyclase]] | [[Category: Adenylate cyclase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: cyclase; beta barrel; dimer]] | [[Category: cyclase; beta barrel; dimer]] | ||
| - | ''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 16:53:13 2008'' |
Revision as of 14:53, 20 March 2008
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| , resolution 1.901Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Adenylate cyclase, with EC number 4.6.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Adenylyl cyclase class iv from Yersinia pestis
Overview
The crystal structure of the class IV adenylyl cyclase (AC) from Yersinia pestis (Yp) is reported at 1.9 A resolution. The class IV AC fold is distinct from the previously described folds for class II and class III ACs. The dimeric AC-IV folds into an antiparallel eight-stranded barrel whose connectivity has been seen in only three previous structures: yeast RNA triphosphatase and two proteins of unknown function from Pyrococcus furiosus and Vibrio parahaemolyticus. Eight highly conserved ionic residues E10, E12, K14, R63, K76, K111, D126, and E136 lie in the barrel core and form the likely binding sites for substrate and divalent cations. A phosphate ion is observed bound to R63, K76, K111, and R113 near the center of the conserved cluster. Unlike the AC-II and AC-III active sites that utilize two-Asp motifs for cation binding, the AC-IV active site is relatively enriched in glutamate and features an ExE motif as its most conserved element. Homologs of Y. pestis AC-IV, including human thiamine triphosphatase, span the three kingdoms of life and delineate an ancient family of phosphonucleotide processing enzymes.
About this Structure
2FJT is a Single protein structure of sequence from Yersinia pestis. Full crystallographic information is available from OCA.
Reference
Structure of the class IV adenylyl cyclase reveals a novel fold., Gallagher DT, Smith NN, Kim SK, Heroux A, Robinson H, Reddy PT, J Mol Biol. 2006 Sep 8;362(1):114-22. Epub 2006 Aug 14. PMID:16905149
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