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| - | [[Image:1tjw.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1tjw| PDB=1tjw | SCENE= }} | | {{STRUCTURE_1tjw| PDB=1tjw | SCENE= }} |
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| - | '''Crystal Structure of T161D Duck Delta 2 Crystallin Mutant with bound argininosuccinate'''
| + | ===Crystal Structure of T161D Duck Delta 2 Crystallin Mutant with bound argininosuccinate=== |
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| - | ==Overview==
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| - | Delta crystallin, a taxon-specific crystallin present in avian eye lenses, is homologous to the urea cycle enzyme ASL (argininosuccinate lyase). Although there are two delta crystallin isoforms in duck lenses, ddeltac1 (duck delta1 crystallin) and ddeltac2 (duck delta2 crystallin), only ddeltac2 is catalytically active. Previous structural studies have suggested that residues Ser283 and His162 in the multi-subunit active site of ddeltac2/ASL are the putative catalytic acid/base, while the highly conserved, positively charged Lys289 is thought to help stabilize the carbanion intermediate. The strict conservation of a small hydroxy-containing residue (Thr or Ser) at position 161 adjacent to the putative catalytic base, as well as its proximity to the substrate in the S283A ddeltac2 enzyme-substrate complex, prompted us to investigate further the role this residue. Structures of the active T161S and inactive T161D ddeltac2 mutants, as well as T161D complexed with argininosuccinate, have been determined to 2.0 A resolution. The structures suggest that a hydroxy group is required at position 161 to help correctly position the side chain of Lys289 and the fumarate moiety of the substrate. Threonine is probably favoured over serine, because the interaction of its methyl group with Leu206 would restrict its conformational flexibility. Residues larger than Thr or Ser interfere with substrate binding, supporting previous suggestions that correct positioning of the substrate's fumarate moiety is essential for catalysis to occur. The presence of the 280s loop (i.e. a loop formed by residues 270-290) in the 'open' conformation suggests that loop closure, thought to be essential for sequestration of the substrate, may be triggered by the formation of the carbanion or aci-carboxylate intermediates, whose charge distribution more closely mimics that of the sulphate ion found in the active-site region of the inactive ddeltac1. The 280s loop in ddeltac1 is in the closed conformation.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15320872}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15320872 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15320872}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Enzyme mechanism]] | | [[Category: Enzyme mechanism]] |
| | [[Category: Eye lens protein]] | | [[Category: Eye lens protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:02:27 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:52:16 2008'' |
Revision as of 01:52, 28 July 2008
Template:STRUCTURE 1tjw
Crystal Structure of T161D Duck Delta 2 Crystallin Mutant with bound argininosuccinate
Template:ABSTRACT PUBMED 15320872
About this Structure
1TJW is a Single protein structure of sequence from Anas platyrhynchos. Full crystallographic information is available from OCA.
Reference
Structural studies of duck delta2 crystallin mutants provide insight into the role of Thr161 and the 280s loop in catalysis., Sampaleanu LM, Codding PW, Lobsanov YD, Tsai M, Smith GD, Horvatin C, Howell PL, Biochem J. 2004 Dec 1;384(Pt 2):437-47. PMID:15320872
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