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| | {{STRUCTURE_1lbm| PDB=1lbm | SCENE= }} | | {{STRUCTURE_1lbm| PDB=1lbm | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF PHOSPHORIBOSYL ANTHRANILATE ISOMERASE (PRAI) IN COMPLEX WITH REDUCED 1-(O-CARBOXYPHENYLAMINO)-1-DEOXYRIBULOSE 5-PHOSPHATE (RCDRP)'''
| + | ===CRYSTAL STRUCTURE OF PHOSPHORIBOSYL ANTHRANILATE ISOMERASE (PRAI) IN COMPLEX WITH REDUCED 1-(O-CARBOXYPHENYLAMINO)-1-DEOXYRIBULOSE 5-PHOSPHATE (RCDRP)=== |
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| - | ==Overview==
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| - | The enzymes N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide isomerase (HisA) and phosphoribosylanthranilate isomerase (TrpF) are sugar isomerases that are involved in histidine and tryptophan biosynthesis, respectively. Both enzymes have the (betaalpha)(8)-barrel fold and catalyze Amadori rearrangements of a thermolabile aminoaldose into the corresponding aminoketose. To identify those amino acids that are essential for catalysis, conserved residues at the active sites of both HisA and TrpF from the hyperthermophile Thermotoga maritima were replaced by site-directed mutagenesis, and the purified variants were investigated by steady-state enzyme kinetics. Aspartate 8, aspartate 127, and threonine 164 appeared to be important for the HisA reaction, whereas cysteine 7 and aspartate 126 appeared to be important for the TrpF reaction. On the basis of these results and the X-ray structure of a complex between TrpF and a bound product analogue, a reaction mechanism involving general acid-base catalysis and a Schiff base intermediate is proposed for both enzymes. A comparison of the HisA and TrpF enzymes from T. maritima and Escherichia coli showed that, at the physiological temperatures of 80 and 37 degrees C, respectively, the enzymes from the hyperthermophile have significantly higher catalytic efficiencies than the corresponding enzymes from mesophiles. These results suggest that HisA and TrpF have similar chemical reaction mechanisms and use the same strategy to prevent the loss of their thermolabile substrates. | + | The line below this paragraph, {{ABSTRACT_PUBMED_12356303}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12356303 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12356303}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Product analogue complex]] | | [[Category: Product analogue complex]] |
| | [[Category: Tryptophan biosynthesis]] | | [[Category: Tryptophan biosynthesis]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:45:47 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 12:16:06 2008'' |
Revision as of 09:16, 2 July 2008
Template:STRUCTURE 1lbm
CRYSTAL STRUCTURE OF PHOSPHORIBOSYL ANTHRANILATE ISOMERASE (PRAI) IN COMPLEX WITH REDUCED 1-(O-CARBOXYPHENYLAMINO)-1-DEOXYRIBULOSE 5-PHOSPHATE (RCDRP)
Template:ABSTRACT PUBMED 12356303
About this Structure
1LBM is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.
Reference
Two (betaalpha)(8)-barrel enzymes of histidine and tryptophan biosynthesis have similar reaction mechanisms and common strategies for protecting their labile substrates., Henn-Sax M, Thoma R, Schmidt S, Hennig M, Kirschner K, Sterner R, Biochemistry. 2002 Oct 8;41(40):12032-42. PMID:12356303
Page seeded by OCA on Wed Jul 2 12:16:06 2008
