2pts: Difference between revisions
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'''Crystal structure of wild type Escherichia coli adenylosuccinate lyase''' | {{Structure | ||
|PDB= 2pts |SIZE=350|CAPTION= <scene name='initialview01'>2pts</scene>, resolution 2.0Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Adenylosuccinate_lyase Adenylosuccinate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.2.2 4.3.2.2] | |||
|GENE= purB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''Crystal structure of wild type Escherichia coli adenylosuccinate lyase''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2PTS is a [ | 2PTS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PTS OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17531264 17531264] | ||
[[Category: Adenylosuccinate lyase]] | [[Category: Adenylosuccinate lyase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: wild-type-selenomethionine substituted]] | [[Category: wild-type-selenomethionine substituted]] | ||
''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 18:17:16 2008'' | ||
Revision as of 19:17, 20 March 2008
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| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | purB (Escherichia coli) | ||||||
| Activity: | Adenylosuccinate lyase, with EC number 4.3.2.2 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of wild type Escherichia coli adenylosuccinate lyase
OverviewOverview
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.
About this StructureAbout this Structure
2PTS is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
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
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