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Crystal structure and reactivity of YbdL from Escherichia coli identify a methionine aminotransferase function.
FEBS Lett. 2004 Jul 30; 571(1-3):141-6.FL

Abstract

The ybdL gene of Escherichia coli codes for a protein of unknown function. Sequence analysis showed moderate homology to several vitamin B(6) dependent enzymes, suggesting that it may bind pyridoxal-5'-phosphate. The structure analysis of YbdL to 2.35 A resolution by protein crystallography verifies that it is a PLP dependent enzyme of fold type I, the typical aspartate aminotransferase fold. The active site contains a bound pyridoxal-5'-phosphate, covalently attached to the conserved active site lysine residue Lys236. The pattern of conserved amino acids in the putative substrate binding pocket of the enzyme reveals that it is most closely related to a hyperthermophilic aromatic residue aminotransferase from the archeon Pyrococcus horikoshii. Activity tests with 10 amino acids as amino-donors reveal, however, a preference for Met, followed by His and Phe, results which can be rationalized by modelization studies.

Authors+Show Affiliations

Architecture et Fonction des Macromolécules Biologiques, UMR 6098, CNRS and Universités d'Aix-Marseille I and II, 31 chemin J. Aiguier, F-13402 Marseille Cedex 20, France.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

15280032

Citation

Dolzan, Manuela, et al. "Crystal Structure and Reactivity of YbdL From Escherichia Coli Identify a Methionine Aminotransferase Function." FEBS Letters, vol. 571, no. 1-3, 2004, pp. 141-6.
Dolzan M, Johansson K, Roig-Zamboni V, et al. Crystal structure and reactivity of YbdL from Escherichia coli identify a methionine aminotransferase function. FEBS Lett. 2004;571(1-3):141-6.
Dolzan, M., Johansson, K., Roig-Zamboni, V., Campanacci, V., Tegoni, M., Schneider, G., & Cambillau, C. (2004). Crystal structure and reactivity of YbdL from Escherichia coli identify a methionine aminotransferase function. FEBS Letters, 571(1-3), 141-6.
Dolzan M, et al. Crystal Structure and Reactivity of YbdL From Escherichia Coli Identify a Methionine Aminotransferase Function. FEBS Lett. 2004 Jul 30;571(1-3):141-6. PubMed PMID: 15280032.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystal structure and reactivity of YbdL from Escherichia coli identify a methionine aminotransferase function. AU - Dolzan,Manuela, AU - Johansson,Kenth, AU - Roig-Zamboni,Véronique, AU - Campanacci,Valérie, AU - Tegoni,Mariella, AU - Schneider,Gunter, AU - Cambillau,Christian, PY - 2004/04/13/received PY - 2004/06/16/revised PY - 2004/06/28/accepted PY - 2004/7/29/pubmed PY - 2004/9/4/medline PY - 2004/7/29/entrez SP - 141 EP - 6 JF - FEBS letters JO - FEBS Lett VL - 571 IS - 1-3 N2 - The ybdL gene of Escherichia coli codes for a protein of unknown function. Sequence analysis showed moderate homology to several vitamin B(6) dependent enzymes, suggesting that it may bind pyridoxal-5'-phosphate. The structure analysis of YbdL to 2.35 A resolution by protein crystallography verifies that it is a PLP dependent enzyme of fold type I, the typical aspartate aminotransferase fold. The active site contains a bound pyridoxal-5'-phosphate, covalently attached to the conserved active site lysine residue Lys236. The pattern of conserved amino acids in the putative substrate binding pocket of the enzyme reveals that it is most closely related to a hyperthermophilic aromatic residue aminotransferase from the archeon Pyrococcus horikoshii. Activity tests with 10 amino acids as amino-donors reveal, however, a preference for Met, followed by His and Phe, results which can be rationalized by modelization studies. SN - 0014-5793 UR - https://www.unboundmedicine.com/medline/citation/15280032/Crystal_structure_and_reactivity_of_YbdL_from_Escherichia_coli_identify_a_methionine_aminotransferase_function_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0014579304008336 DB - PRIME DP - Unbound Medicine ER -