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| | {{STRUCTURE_1dqu| PDB=1dqu | SCENE= }} | | {{STRUCTURE_1dqu| PDB=1dqu | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF THE ISOCITRATE LYASE FROM ASPERGILLUS NIDULANS'''
| + | ===CRYSTAL STRUCTURE OF THE ISOCITRATE LYASE FROM ASPERGILLUS NIDULANS=== |
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| - | ==Overview==
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| - | BACKGROUND: Isocitrate lyase catalyses the first committed step of the carbon-conserving glyoxylate bypass, the Mg(2+)-dependent reversible cleavage of isocitrate into succinate and glyoxylate. This metabolic pathway is an inviting target for the control of a number of diseases, because the enzymes involved in this cycle have been identified in many pathogens including Mycobacterium leprae and Leishmania. RESULTS: As part of a programme of rational drug design the structure of the tetrameric Aspergillus nidulans isocitrate lyase and its complex with glyoxylate and a divalent cation have been solved to 2.8 A resolution using X-ray diffraction. Each subunit comprises two domains, one of which adopts a folding pattern highly reminiscent of the triose phosphate isomerase (TIM) barrel. A 'knot' between subunits observed in the three-dimensional structure, involving residues towards the C terminus, implies that tetramer assembly involves considerable flexibility in this part of the protein. CONCLUSIONS: Difference Fourier analysis together with the pattern of sequence conservation has led to the identification of both the glyoxylate and metal binding sites and implicates the C-terminal end of the TIM barrel as the active site, which is consistent with studies of other enzymes with this fold. Two disordered regions of the polypeptide chain lie close to the active site, one of which includes a critical cysteine residue suggesting that conformational rearrangements are essential for catalysis. Structural similarities between isocitrate lyase and both PEP mutase and enzymes belonging to the enolase superfamily suggest possible relationships in aspects of the mechanism.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10801489}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10801489 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10801489}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Weeradechapon, K.]] | | [[Category: Weeradechapon, K.]] |
| | [[Category: Beta barrel]] | | [[Category: Beta barrel]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:10:06 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:29:00 2008'' |
Revision as of 20:29, 30 June 2008
Template:STRUCTURE 1dqu
CRYSTAL STRUCTURE OF THE ISOCITRATE LYASE FROM ASPERGILLUS NIDULANS
Template:ABSTRACT PUBMED 10801489
About this Structure
1DQU is a Single protein structure of sequence from Emericella nidulans. Full crystallographic information is available from OCA.
Reference
The crystal structure and active site location of isocitrate lyase from the fungus Aspergillus nidulans., Britton K, Langridge S, Baker PJ, Weeradechapon K, Sedelnikova SE, De Lucas JR, Rice DW, Turner G, Structure. 2000 Apr 15;8(4):349-62. PMID:10801489
Page seeded by OCA on Mon Jun 30 23:29:00 2008
