2ptq: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,494 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,494 edits
No edit summary
Line 1: Line 1:
[[Image:2ptq.jpg|left|200px]]
{{Seed}}
[[Image:2ptq.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2ptq|  PDB=2ptq  |  SCENE=  }}  
{{STRUCTURE_2ptq|  PDB=2ptq  |  SCENE=  }}  


'''Crystal structure of Escherichia coli adenylosuccinate lyase mutant H171N with bound AMP and fumarate'''
===Crystal structure of Escherichia coli adenylosuccinate lyase mutant H171N with bound AMP and fumarate===




==Overview==
<!--  
Adenylosuccinate lyase (ADL) catalyzes the breakdown of 5-aminoimidazole- (N-succinylocarboxamide) ribotide (SAICAR) to 5-aminoimidazole-4-carboxamide ribotide (AICAR) and fumarate, and of adenylosuccinate (ADS) to adenosine monophosphate (AMP) and fumarate in the de novo purine biosynthetic pathway. ADL belongs to the argininosuccinate lyase (ASL)/fumarase C superfamily of enzymes. Members of this family share several common features including: a mainly alpha-helical, homotetrameric structure; three regions of highly conserved amino acid residues; and a general acid-base catalytic mechanism with the overall beta-elimination of fumarate as a product. The crystal structures of wild-type Escherichia coli ADL (ec-ADL), and mutant-substrate (H171A-ADS) and -product (H171N-AMP.FUM) complexes have been determined to 2.0, 1.85, and 2.0 A resolution, respectively. The H171A-ADS and H171N-AMP.FUM structures provide the first detailed picture of the ADL active site, and have enabled the precise identification of substrate binding and putative catalytic residues. Contrary to previous suggestions, the ec-ADL structures implicate S295 and H171 in base and acid catalysis, respectively. Furthermore, structural alignments of ec-ADL with other superfamily members suggest for the first time a large conformational movement of the flexible C3 loop (residues 287-303) in ec-ADL upon substrate binding and catalysis, resulting in its closure over the active site. This loop movement has been observed in other superfamily enzymes, and has been proposed to be essential for catalysis. The ADL catalytic mechanism is re-examined in light of the results presented here.
The line below this paragraph, {{ABSTRACT_PUBMED_17531264}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 17531264 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_17531264}}


==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Adenylosuccinate lyase]]
[[Category: Adenylosuccinate lyase]]
[[Category: Mutant-product complex]]
[[Category: Mutant-product complex]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 13:47:25 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:12:28 2008''

Revision as of 00:12, 28 July 2008

File:2ptq.png

Template:STRUCTURE 2ptq

Crystal structure of Escherichia coli adenylosuccinate lyase mutant H171N with bound AMP and fumarate

Template:ABSTRACT PUBMED 17531264

About this Structure

2PTQ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Substrate and product complexes of Escherichia coli adenylosuccinate lyase provide new insights into the enzymatic mechanism., Tsai M, Koo J, Yip P, Colman RF, Segall ML, Howell PL, J Mol Biol. 2007 Jul 13;370(3):541-54. Epub 2007 May 4. PMID:17531264

Page seeded by OCA on Mon Jul 28 03:12:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2ptq&oldid=678309"