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The role of evolutionarily conserved hydrophobic contacts in the quaternary structure stability of Escherichia coli serine hydroxymethyltransferase.
FEBS J. 2009 Jan; 276(1):132-43.FJ

Abstract

Pyridoxal 5'-phosphate-dependent enzymes may be grouped into five structural superfamilies of proteins, corresponding to as many fold types. The fold type I is by far the largest and most investigated group. An important feature of this fold, which is characterized by the presence of two domains, appears to be the existence of three clusters of evolutionarily conserved hydrophobic contacts. Although two of these clusters are located in the central cores of the domains and presumably stabilize their scaffold, allowing the correct alignment of the residues involved in cofactor and substrate binding, the role of the third cluster is much less evident. A site-directed mutagenesis approach was used to carry out a model study on the importance of the third cluster in the structure of a well characterized member of the fold type I group, serine hydroxymethyltransferase from Escherichia coli. The experimental results obtained indicated that the cluster plays a crucial role in the stabilization of the quaternary, native assembly of the enzyme, although it is not located at the subunit interface. The analysis of the crystal structure of serine hydroxymethyltransferase suggested that this stabilizing effect may be due to the strict structural relation between the cluster and two polypeptide loops, which, in fold type I enzymes, mediate the interactions between the subunits and are involved in cofactor binding, substrate binding and catalysis.

Authors+Show Affiliations

Dipartimento di Scienze Biochimiche A. Rossi Fanelli, Sapienza Università di Roma, Italy.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

19019081

Citation

Florio, Rita, et al. "The Role of Evolutionarily Conserved Hydrophobic Contacts in the Quaternary Structure Stability of Escherichia Coli Serine Hydroxymethyltransferase." The FEBS Journal, vol. 276, no. 1, 2009, pp. 132-43.
Florio R, Chiaraluce R, Consalvi V, et al. The role of evolutionarily conserved hydrophobic contacts in the quaternary structure stability of Escherichia coli serine hydroxymethyltransferase. FEBS J. 2009;276(1):132-43.
Florio, R., Chiaraluce, R., Consalvi, V., Paiardini, A., Catacchio, B., Bossa, F., & Contestabile, R. (2009). The role of evolutionarily conserved hydrophobic contacts in the quaternary structure stability of Escherichia coli serine hydroxymethyltransferase. The FEBS Journal, 276(1), 132-43. https://doi.org/10.1111/j.1742-4658.2008.06761.x
Florio R, et al. The Role of Evolutionarily Conserved Hydrophobic Contacts in the Quaternary Structure Stability of Escherichia Coli Serine Hydroxymethyltransferase. FEBS J. 2009;276(1):132-43. PubMed PMID: 19019081.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The role of evolutionarily conserved hydrophobic contacts in the quaternary structure stability of Escherichia coli serine hydroxymethyltransferase. AU - Florio,Rita, AU - Chiaraluce,Roberta, AU - Consalvi,Valerio, AU - Paiardini,Alessandro, AU - Catacchio,Bruno, AU - Bossa,Francesco, AU - Contestabile,Roberto, PY - 2008/11/21/entrez PY - 2008/11/21/pubmed PY - 2009/2/4/medline SP - 132 EP - 43 JF - The FEBS journal JO - FEBS J VL - 276 IS - 1 N2 - Pyridoxal 5'-phosphate-dependent enzymes may be grouped into five structural superfamilies of proteins, corresponding to as many fold types. The fold type I is by far the largest and most investigated group. An important feature of this fold, which is characterized by the presence of two domains, appears to be the existence of three clusters of evolutionarily conserved hydrophobic contacts. Although two of these clusters are located in the central cores of the domains and presumably stabilize their scaffold, allowing the correct alignment of the residues involved in cofactor and substrate binding, the role of the third cluster is much less evident. A site-directed mutagenesis approach was used to carry out a model study on the importance of the third cluster in the structure of a well characterized member of the fold type I group, serine hydroxymethyltransferase from Escherichia coli. The experimental results obtained indicated that the cluster plays a crucial role in the stabilization of the quaternary, native assembly of the enzyme, although it is not located at the subunit interface. The analysis of the crystal structure of serine hydroxymethyltransferase suggested that this stabilizing effect may be due to the strict structural relation between the cluster and two polypeptide loops, which, in fold type I enzymes, mediate the interactions between the subunits and are involved in cofactor binding, substrate binding and catalysis. SN - 1742-4658 UR - https://www.unboundmedicine.com/medline/citation/19019081/The_role_of_evolutionarily_conserved_hydrophobic_contacts_in_the_quaternary_structure_stability_of_Escherichia_coli_serine_hydroxymethyltransferase_ L2 - https://doi.org/10.1111/j.1742-4658.2008.06761.x DB - PRIME DP - Unbound Medicine ER -