Filling out the structural map of the NTF2-like superfamily.

Filling out the structural map of the NTF2-like superfamily.
复制标题

DOI:
10.1186/1471-2105-14-327
复制
发表时间:
2013-11-19
期刊:
影响因子:
3
通讯作者:
Aravind L
Aravind L
中科院分区:
生物学4区
文献类型:
--
作者:
Eberhardt RY;Chang Y;Bateman A;Murzin AG;Axelrod HL;Hwang WC;Aravind L

文献摘要

参考文献

被引文献

相似文献

NTF2 样超家族是一组具有共同折叠的多功能蛋白质结构域。这些结构域的序列非常多样化,并且它们没有共同的序列基序。这些结构域在它们所在的蛋白质中发挥着一系列不同的功能,包括催化和非催化版本。属于这种多样化超家族的蛋白质结构域的功能线索可以通过对蛋白质和发现它们的生物体的分析来收集。在这里,我们描述了主要在细菌中发现的三个功能未知的蛋白质结构域:DUF3828、DUF3887 和 DUF4878。每个结构域的代表结构:来自多形拟杆菌(菌株 VPI-5482)的 BT_3511 [PDB:3KZT]、来自空肠弯曲杆菌亚种的 Cj0202c。空肠杆菌血清型 O:2(菌株 NCTC 11168)[PDB:3K7C]、rumgna_01855)和来自 gnavus 瘤胃球菌(菌株 ATCC 29149)[PDB:4HYZ] 的 RUMGNA_01855 已通过 X 射线晶体学解析。这三个结构域结构相似,均属于 NTF2 样超家族。尽管这些结构域的功能目前仍不清楚,但我们的分析使我们能够提出有关其作用的假设。我们对这三个蛋白质结构域的分析表明潜在的非催化配体结合作用。这可以调节与它们组合在同一多肽中或通过操纵子连接的结构域的活性,例如信号结构域(例如丝氨酸/苏氨酸蛋白激酶)、肽聚糖加工水解酶(例如NlpC/P60肽酶)或核酸结合结构域(例如Zn带)。
The NTF2-like superfamily is a versatile group of protein domains sharing a common fold. The sequences of these domains are very diverse and they share no common sequence motif. These domains serve a range of different functions within the proteins in which they are found, including both catalytic and non-catalytic versions. Clues to the function of protein domains belonging to such a diverse superfamily can be gleaned from analysis of the proteins and organisms in which they are found. Here we describe three protein domains of unknown function found mainly in bacteria: DUF3828, DUF3887 and DUF4878. Structures of representatives of each of these domains: BT_3511 from Bacteroides thetaiotaomicron (strain VPI-5482) [PDB:3KZT], Cj0202c from Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168) [PDB:3K7C], rumgna_01855) and RUMGNA_01855 from Ruminococcus gnavus (strain ATCC 29149) [PDB:4HYZ] have been solved by X-ray crystallography. All three domains are similar in structure and all belong to the NTF2-like superfamily. Although the function of these domains remains unknown at present, our analysis enables us to present a hypothesis concerning their role. Our analysis of these three protein domains suggests a potential non-catalytic ligand-binding role. This may regulate the activities of domains with which they are combined in the same polypeptide or via operonic linkages, such as signaling domains (e.g. serine/threonine protein kinase), peptidoglycan-processing hydrolases (e.g. NlpC/P60 peptidases) or nucleic acid binding domains (e.g. Zn-ribbons).
DOI: 10.1107/s0907444905036693
发表时间: 2006-01-01
影响因子: 2.2
作者:
Evans, P
通讯作者: Evans, P
DOI: 10.1107/s0907444904019158
发表时间: 2004-12-01
影响因子: 2.2
作者:
Emsley, P;Cowtan, K
通讯作者: Cowtan, K
DOI: 10.1093/emboj/cdg275
发表时间: 2003-06-02
期刊: EMBO JOURNAL
影响因子: 11.4
作者:
Arand, M;Hallberg, BM;Mowbray, SL
通讯作者: Mowbray, SL
DOI: 10.1107/s1744309110038212
发表时间: 2010-10-01
影响因子: 0.9
作者:
Elsliger, Marc-Andre;Deacon, Ashley M.;Wilson, Ian A.
通讯作者: Wilson, Ian A.
DOI: 10.1073/pnas.142413399
发表时间: 2002-09-03
影响因子: 11.1
作者:
Lesley, SA;Kuhn, P;Stevens, RC
通讯作者: Stevens, RC