1m8p: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
[[Image:1m8p.gif|left|200px]]
{{Seed}}
[[Image:1m8p.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1m8p|  PDB=1m8p  |  SCENE=  }}  
{{STRUCTURE_1m8p|  PDB=1m8p  |  SCENE=  }}  


'''Crystal Structure of P. chrysogenum ATP Sulfurylase in the T-state'''
===Crystal Structure of P. chrysogenum ATP Sulfurylase in the T-state===




==Overview==
<!--
The structure of the cooperative hexameric enzyme ATP sulfurylase from Penicillium chrysogenum bound to its allosteric inhibitor, 3'-phosphoadenosine-5'-phosphosulfate (PAPS), was determined to 2.6 A resolution. This structure represents the low substrate-affinity T-state conformation of the enzyme. Comparison with the high substrate-affinity R-state structure reveals that a large rotational rearrangement of domains occurs as a result of the R-to-T transition. The rearrangement is accompanied by the 17 A movement of a 10-residue loop out of the active site region, resulting in an open, product release-like structure of the catalytic domain. Binding of PAPS is proposed to induce the allosteric transition by destabilizing an R-state-specific salt linkage between Asp 111 in an N-terminal domain of one subunit and Arg 515 in the allosteric domain of a trans-triad subunit. Disrupting this salt linkage by site-directed mutagenesis induces cooperative inhibition behavior in the absence of an allosteric effector, confirming the role of these two residues.
The line below this paragraph, {{ABSTRACT_PUBMED_12426581}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 12426581 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_12426581}}


==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Rossmann fold]]
[[Category: Rossmann fold]]
[[Category: T-state]]
[[Category: T-state]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:46:09 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:27:03 2008''

Revision as of 20:27, 2 July 2008

File:1m8p.png

Template:STRUCTURE 1m8p

Crystal Structure of P. chrysogenum ATP Sulfurylase in the T-state

Template:ABSTRACT PUBMED 12426581

About this Structure

1M8P is a Single protein structure of sequence from Penicillium chrysogenum. Full crystallographic information is available from OCA.

Reference

Allosteric inhibition via R-state destabilization in ATP sulfurylase from Penicillium chrysogenum., MacRae IJ, Segel IH, Fisher AJ, Nat Struct Biol. 2002 Dec;9(12):945-9. PMID:12426581

Page seeded by OCA on Wed Jul 2 23:27:03 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1m8p&oldid=629451"