Literature DB >> 14734322

PGTdb: a database providing growth temperatures of prokaryotes.

Shir-Ly Huang1, Li-Cheng Wu, Han-Kuen Liang, Kuan-Ting Pan, Jorng-Tzong Horng, Ming-Tat Ko.   

Abstract

UNLABELLED: Included in Prokaryotic Growth Temperature database (PGTdb) are a total of 1334 temperature data from 1072 prokaryotic organisms, Bacteria and Archaea: PGTdb integrates microbial growth temperature data from literature survey with their nucleotide/protein sequence and protein structure data from related databases. A direct correlation is observed between the average growth temperature of an organism and the melting temperature of proteins from the organism. Therefore, this database is useful not only for microbiologists to obtain cultivation condition, but also for biochemists and structure biologists to study the correlation between protein sequences/structures and their thermostability. In addition, the taxonomy and ribosomal RNA sequence(s) of an organism are linked through NCBI Taxonomy and the Ribosomal RNA Operon Copy Number Database umdb, respectively. PGTdb is the only integrated database on the Internet to provide the growth temperature data of the prokaryotes and the combined information of their nucleotide/protein sequences, protein structures, taxonomy and phylogeny. AVAILABILITY: http://pgtdb.csie.ncu.edu.tw

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Year:  2004        PMID: 14734322     DOI: 10.1093/bioinformatics/btg403

Source DB:  PubMed          Journal:  Bioinformatics        ISSN: 1367-4803            Impact factor:   6.937


  28 in total

1.  Distance-dependent statistical potentials for discriminating thermophilic and mesophilic proteins.

Authors:  Yunqi Li; Jianwen Fang
Journal:  Biochem Biophys Res Commun       Date:  2010-05-06       Impact factor: 3.575

2.  Comparison of the structural basis for thermal stability between archaeal and bacterial proteins.

Authors:  Yanrui Ding; Yujie Cai; Yonggang Han; Bingqiang Zhao
Journal:  Extremophiles       Date:  2011-10-21       Impact factor: 2.395

3.  Prokaryotes that grow optimally in acid have purine-poor codons in long open reading frames.

Authors:  Feng-Hsu Lin; Donald R Forsdyke
Journal:  Extremophiles       Date:  2006-09-07       Impact factor: 2.395

4.  The role of semidisorder in temperature adaptation of bacterial FlgM proteins.

Authors:  Jihua Wang; Yuedong Yang; Zanxia Cao; Zhixiu Li; Huiying Zhao; Yaoqi Zhou
Journal:  Biophys J       Date:  2013-12-03       Impact factor: 4.033

5.  Compositional properties and thermal adaptation of SRP-RNA in bacteria and archaea.

Authors:  Francisco Miralles
Journal:  J Mol Evol       Date:  2010-01-13       Impact factor: 2.395

6.  Temperature dependence of the flexibility of thermophilic and mesophilic flavoenzymes of the nitroreductase fold.

Authors:  Eric D Merkley; William W Parson; Valerie Daggett
Journal:  Protein Eng Des Sel       Date:  2010-01-18       Impact factor: 1.650

7.  Amino acid contacts in proteins adapted to different temperatures: hydrophobic interactions and surface charges play a key role.

Authors:  Gisle Saelensminde; Øyvind Halskau; Inge Jonassen
Journal:  Extremophiles       Date:  2008-09-30       Impact factor: 2.395

8.  Compositional and structural features related to thermal stability in the archaea SRP19 and SRP54 signal recognition particle proteins.

Authors:  Francisco Miralles
Journal:  J Mol Evol       Date:  2011-04-20       Impact factor: 2.395

9.  Parallel evolution of transcriptome architecture during genome reorganization.

Authors:  Sung Ho Yoon; David J Reiss; J Christopher Bare; Dan Tenenbaum; Min Pan; Joseph Slagel; Robert L Moritz; Sujung Lim; Murray Hackett; Angeli Lal Menon; Michael W W Adams; Adam Barnebey; Steven M Yannone; John A Leigh; Nitin S Baliga
Journal:  Genome Res       Date:  2011-07-12       Impact factor: 9.043

10.  Reduction in structural disorder and functional complexity in the thermal adaptation of prokaryotes.

Authors:  Prasad V Burra; Lajos Kalmar; Peter Tompa
Journal:  PLoS One       Date:  2010-08-11       Impact factor: 3.240

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