Protein Family Models

This domain is found C-terminal in a number of thiolases and their homologues. Thiolases are essential CoA-dependent enzymes in lipid metabolism. This domain folds into a four-stranded antiparallel beta-sheet with helices packed on one side. Paper describing PDB structure 1afw. [1]. 9402066. The 1.8 A crystal structure of the dimeric peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: implications for substrate binding and reaction mechanism. Mathieu M, Modis Y, Zeelen JP, Engel CK, Abagyan RA, Ahlberg A, Rasmussen B, Lamzin VS, Kunau WH, Wierenga RK;. J Mol Biol 1997;273:714-728. Paper describing PDB structure 1dlu. [2]. 10764581. Crystallographic analysis of the reaction pathway of Zoogloea ramigera biosynthetic thiolase. Modis Y, Wierenga RK;. J Mol Biol. 2000;297:1171-1182. Paper describing PDB structure 1hzp. [3]. 11278743. Crystal structure of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III. Scarsdale JN, Kazanina G, He X, Reynolds KA, Wright HT;. J Biol Chem. 2001;276:20516-20522. Paper describing PDB structure 1m1m. [4]. 16040614. Probing the mechanism of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III mtFabH: factors influencing catalysis and substrate specificity. Brown AK, Sridharan S, Kremer L, Lindenberg S, Dover LG, Sacchettini JC, Besra GS;. J Biol Chem. 2005;280:32539-32547. Paper describing PDB structure 1m1o. [5]. 12501183. The catalytic cycle of biosynthetic thiolase: a conformational journey of an acetyl group through four binding modes and two oxyanion holes. Kursula P, Ojala J, Lambeir AM, Wierenga RK;. Biochemistry. 2002;41:1. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

This domain has no known function and is found in conserved hypothetical archaeal and bacterial proteins. The domain is duplicated in Swiss:O53566. The structure of a DUF35 representative reveals two long N-terminal helices followed by a rubredoxin-like zinc ribbon domain represented in this family and a C-terminal OB fold domain. Zinc is chelated by the four conserved cysteines in the alignment. (from Pfam)

Date:

2024-08-14

The structure of a DUF35 representative reveals two long N-terminal helices followed by a rubredoxin-like zinc ribbon domain and a C-terminal OB fold domain represented in this entry. OB-folds are frequently found to bind nucleic acids suggesting this domain might bind to DNA or RNA (Topsan http://www.topsan.org/). Genomic context shows it to be adjacent to acyl-CoA transferase (http:/www.microbesonline.org/). [1]. 20944206. The structure of SSO2064, the first representative of Pfam family PF01796, reveals a novel two-domain zinc-ribbon OB-fold architecture with a potential acyl-CoA-binding role. Krishna SS, Aravind L, Bakolitsa C, Caruthers J, Carlton D, Miller MD, Abdubek P, Astakhova T, Axelrod HL, Chiu HJ, Clayton T, Deller MC, Duan L, Feuerhelm J, Grant JC, Han GW, Jaroszewski L, Jin KK, Klock HE, Knuth MW, Kumar A, Marciano D, McMullan D, Morse AT, Nigoghossian E, Okach L, Reyes R, Rife CL, van den Bedem H, Weekes D, Xu Q, Hodgson KO, Wooley J, Elsliger MA, Deacon AM, Godzik A, Lesley SA, Wilson IA;. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010;66:1160-1166. [2]. 23793631. Haloarchaeal-type beta-ketothiolases involved in Poly(3-hydroxybutyrate-co-3-hydroxyvalerate) synthesis in Haloferax mediterranei. Hou J, Feng B, Han J, Liu H, Zhao D, Zhou J, Xiang H;. Appl Environ Microbiol. 2013;79:5104-5111. (from Pfam)

Date:

2024-10-16

protein containing domains DUF35_N, OB_aCoA_assoc, and SCP-x_thiolase

Date:

2017-03-02