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1g8m
From Proteopedia
(New page: 200px<br /><applet load="1g8m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g8m, resolution 1.75Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1g8m.jpg|left|200px]]<br /><applet load="1g8m" size=" | + | [[Image:1g8m.jpg|left|200px]]<br /><applet load="1g8m" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1g8m, resolution 1.75Å" /> | caption="1g8m, resolution 1.75Å" /> | ||
'''CRYSTAL STRUCTURE OF AVIAN ATIC, A BIFUNCTIONAL TRANSFORMYLASE AND CYCLOHYDROLASE ENZYME IN PURINE BIOSYNTHESIS AT 1.75 ANG. RESOLUTION'''<br /> | '''CRYSTAL STRUCTURE OF AVIAN ATIC, A BIFUNCTIONAL TRANSFORMYLASE AND CYCLOHYDROLASE ENZYME IN PURINE BIOSYNTHESIS AT 1.75 ANG. RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | ATIC, the product of the purH gene, is a 64 kDa bifunctional enzyme that | + | ATIC, the product of the purH gene, is a 64 kDa bifunctional enzyme that possesses the final two activities in de novo purine biosynthesis, AICAR transformylase and IMP cyclohydrolase. The crystal structure of avian ATIC has been determined to 1.75 A resolution by the MAD method using a Se-methionine modified enzyme. ATIC forms an intertwined dimer with an extensive interface of approximately 5,000 A(2) per monomer. Each monomer is composed of two novel, separate functional domains. The N-terminal domain (up to residue 199) is responsible for the IMPCH activity, whereas the AICAR Tfase activity resides in the C-terminal domain (200-593). The active sites of the IMPCH and AICAR Tfase domains are approximately 50 A apart, with no structural evidence of a tunnel connecting the two active sites. The crystal structure of ATIC provides a framework to probe both catalytic mechanisms and to design specific inhibitors for use in cancer chemotherapy and inflammation. |
==About this Structure== | ==About this Structure== | ||
| - | 1G8M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with K and G as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1G8M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=K:'>K</scene> and <scene name='pdbligand=G:'>G</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G8M OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Beardsley, G | + | [[Category: Beardsley, G P.]] |
| - | [[Category: Benkovic, S | + | [[Category: Benkovic, S J.]] |
| - | [[Category: Greasley, S | + | [[Category: Greasley, S E.]] |
[[Category: Horton, P.]] | [[Category: Horton, P.]] | ||
| - | [[Category: Wilson, I | + | [[Category: Wilson, I A.]] |
[[Category: G]] | [[Category: G]] | ||
[[Category: K]] | [[Category: K]] | ||
| Line 24: | Line 24: | ||
[[Category: homodimer]] | [[Category: homodimer]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:47:31 2008'' |
Revision as of 10:47, 21 February 2008
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CRYSTAL STRUCTURE OF AVIAN ATIC, A BIFUNCTIONAL TRANSFORMYLASE AND CYCLOHYDROLASE ENZYME IN PURINE BIOSYNTHESIS AT 1.75 ANG. RESOLUTION
Overview
ATIC, the product of the purH gene, is a 64 kDa bifunctional enzyme that possesses the final two activities in de novo purine biosynthesis, AICAR transformylase and IMP cyclohydrolase. The crystal structure of avian ATIC has been determined to 1.75 A resolution by the MAD method using a Se-methionine modified enzyme. ATIC forms an intertwined dimer with an extensive interface of approximately 5,000 A(2) per monomer. Each monomer is composed of two novel, separate functional domains. The N-terminal domain (up to residue 199) is responsible for the IMPCH activity, whereas the AICAR Tfase activity resides in the C-terminal domain (200-593). The active sites of the IMPCH and AICAR Tfase domains are approximately 50 A apart, with no structural evidence of a tunnel connecting the two active sites. The crystal structure of ATIC provides a framework to probe both catalytic mechanisms and to design specific inhibitors for use in cancer chemotherapy and inflammation.
About this Structure
1G8M is a Single protein structure of sequence from Gallus gallus with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of a bifunctional transformylase and cyclohydrolase enzyme in purine biosynthesis., Greasley SE, Horton P, Ramcharan J, Beardsley GP, Benkovic SJ, Wilson IA, Nat Struct Biol. 2001 May;8(5):402-6. PMID:11323713
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