1cjv
From Proteopedia
(New page: 200px<br /><applet load="1cjv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cjv, resolution 3.00Å" /> '''COMPLEX OF GS-ALPHA ...) |
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| - | [[Image:1cjv.gif|left|200px]]<br /><applet load="1cjv" size=" | + | [[Image:1cjv.gif|left|200px]]<br /><applet load="1cjv" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1cjv, resolution 3.00Å" /> | caption="1cjv, resolution 3.00Å" /> | ||
'''COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE: COMPLEX WITH BETA-L-2',3'-DIDEOXYATP, MG, AND ZN'''<br /> | '''COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE: COMPLEX WITH BETA-L-2',3'-DIDEOXYATP, MG, AND ZN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Adenylyl cyclase (AC) converts adenosine triphosphate (ATP) to cyclic | + | Adenylyl cyclase (AC) converts adenosine triphosphate (ATP) to cyclic adenosine monophosphate, a ubiquitous second messenger that regulates many cellular functions. Recent structural studies have revealed much about the structure and function of mammalian AC but have not fully defined its active site or catalytic mechanism. Four crystal structures were determined of the catalytic domains of AC in complex with two different ATP analogs and various divalent metal ions. These structures provide a model for the enzyme-substrate complex and conclusively demonstrate that two metal ions bind in the active site. The similarity of the active site of AC to those of DNA polymerases suggests that the enzymes catalyze phosphoryl transfer by the same two-metal-ion mechanism and likely have evolved from a common ancestor. |
==About this Structure== | ==About this Structure== | ||
| - | 1CJV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus], [http://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with MG, CL, ZN, GSP, FOK, DAD and MES 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:// | + | 1CJV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus], [http://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=GSP:'>GSP</scene>, <scene name='pdbligand=FOK:'>FOK</scene>, <scene name='pdbligand=DAD:'>DAD</scene> and <scene name='pdbligand=MES:'>MES</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=1CJV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
| - | [[Category: Sprang, S | + | [[Category: Sprang, S R.]] |
| - | [[Category: Tesmer, J | + | [[Category: Tesmer, J J.G.]] |
[[Category: CL]] | [[Category: CL]] | ||
[[Category: DAD]] | [[Category: DAD]] | ||
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[[Category: signal transducing protein]] | [[Category: signal transducing protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:06:46 2008'' |
Revision as of 10:06, 21 February 2008
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COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE: COMPLEX WITH BETA-L-2',3'-DIDEOXYATP, MG, AND ZN
Overview
Adenylyl cyclase (AC) converts adenosine triphosphate (ATP) to cyclic adenosine monophosphate, a ubiquitous second messenger that regulates many cellular functions. Recent structural studies have revealed much about the structure and function of mammalian AC but have not fully defined its active site or catalytic mechanism. Four crystal structures were determined of the catalytic domains of AC in complex with two different ATP analogs and various divalent metal ions. These structures provide a model for the enzyme-substrate complex and conclusively demonstrate that two metal ions bind in the active site. The similarity of the active site of AC to those of DNA polymerases suggests that the enzymes catalyze phosphoryl transfer by the same two-metal-ion mechanism and likely have evolved from a common ancestor.
About this Structure
1CJV is a Protein complex structure of sequences from Bos taurus, Canis lupus familiaris and Rattus norvegicus with , , , , , and as ligands. Active as Adenylate cyclase, with EC number 4.6.1.1 Full crystallographic information is available from OCA.
Reference
Two-metal-Ion catalysis in adenylyl cyclase., Tesmer JJ, Sunahara RK, Johnson RA, Gosselin G, Gilman AG, Sprang SR, Science. 1999 Jul 30;285(5428):756-60. PMID:10427002
Page seeded by OCA on Thu Feb 21 12:06:46 2008
Categories: Adenylate cyclase | Bos taurus | Canis lupus familiaris | Protein complex | Rattus norvegicus | Sprang, S R. | Tesmer, J J.G. | CL | DAD | FOK | GSP | MES | MG | ZN | Complex (lyase/hydrolase) | Cyclase | Effector enzyme | Hydrolase | Signal transducing protein
