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The structure of serine hydroxymethyltransferase as modeled by homology and validated by site-directed mutagenesis.
Protein Sci. 1998 Sep; 7(9):1976-82.PS

Abstract

We describe a model for the three-dimensional structure of E. coli serine hydroxymethyltransferase based on its sequence homology with other PLP enzymes of the alpha-family and whose tertiary structures are known. The model suggests that certain amino acid residues at the putative active site of the enzyme can adopt specific roles in the catalytic mechanism. These proposals were supported by analysis of the properties of a number of site-directed mutants. New active site features are also proposed for further experimental testing.

Authors+Show Affiliations

Dipartimento di Scienze Biochimiche A. Rossi Fanelli and Centro di Biologia Molecolare del CNR, Università La Sapienza, Roma, Italy.No 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

9761478

Citation

Pascarella, S, et al. "The Structure of Serine Hydroxymethyltransferase as Modeled By Homology and Validated By Site-directed Mutagenesis." Protein Science : a Publication of the Protein Society, vol. 7, no. 9, 1998, pp. 1976-82.
Pascarella S, Angelaccio S, Contestabile R, et al. The structure of serine hydroxymethyltransferase as modeled by homology and validated by site-directed mutagenesis. Protein Sci. 1998;7(9):1976-82.
Pascarella, S., Angelaccio, S., Contestabile, R., Delle Fratte, S., Di Salvo, M., & Bossa, F. (1998). The structure of serine hydroxymethyltransferase as modeled by homology and validated by site-directed mutagenesis. Protein Science : a Publication of the Protein Society, 7(9), 1976-82.
Pascarella S, et al. The Structure of Serine Hydroxymethyltransferase as Modeled By Homology and Validated By Site-directed Mutagenesis. Protein Sci. 1998;7(9):1976-82. PubMed PMID: 9761478.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The structure of serine hydroxymethyltransferase as modeled by homology and validated by site-directed mutagenesis. AU - Pascarella,S, AU - Angelaccio,S, AU - Contestabile,R, AU - Delle Fratte,S, AU - Di Salvo,M, AU - Bossa,F, PY - 1998/10/7/pubmed PY - 1998/10/7/medline PY - 1998/10/7/entrez SP - 1976 EP - 82 JF - Protein science : a publication of the Protein Society JO - Protein Sci VL - 7 IS - 9 N2 - We describe a model for the three-dimensional structure of E. coli serine hydroxymethyltransferase based on its sequence homology with other PLP enzymes of the alpha-family and whose tertiary structures are known. The model suggests that certain amino acid residues at the putative active site of the enzyme can adopt specific roles in the catalytic mechanism. These proposals were supported by analysis of the properties of a number of site-directed mutants. New active site features are also proposed for further experimental testing. SN - 0961-8368 UR - https://www.unboundmedicine.com/medline/citation/9761478/The_structure_of_serine_hydroxymethyltransferase_as_modeled_by_homology_and_validated_by_site_directed_mutagenesis_ L2 - https://doi.org/10.1002/pro.5560070913 DB - PRIME DP - Unbound Medicine ER -