2EXD
The solution structure of the C-terminal domain of a nfeD homolog from Pyrococcus horikoshii
Summary for 2EXD
| Entry DOI | 10.2210/pdb2exd/pdb |
| NMR Information | BMRB: 10118 |
| Descriptor | nfeD short homolog (1 entity in total) |
| Functional Keywords | nfed, membrane protein |
| Biological source | Pyrococcus horikoshii |
| Total number of polymer chains | 1 |
| Total formula weight | 9203.57 |
| Authors | Kuwahara, Y.,Ohno, A.,Morii, T.,Tochio, H.,Shirakawa, M.,Hiroaki, H. (deposition date: 2005-11-08, release date: 2006-12-12, Last modification date: 2024-05-01) |
| Primary citation | Kuwahara, Y.,Ohno, A.,Morii, T.,Yokoyama, H.,Matsui, I.,Tochio, H.,Shirakawa, M.,Hiroaki, H. The solution structure of the C-terminal domain of NfeD reveals a novel membrane-anchored OB-fold. Protein Sci., 17:1915-1924, 2008 Cited by PubMed Abstract: Nodulation formation efficiency D (NfeD) is a member of a class of membrane-anchored ClpP-class proteases. There is a second class of NfeD homologs that lack the ClpP domain. The genes of both NfeD classes usually are part of an operon that also contains a gene for a prokaryotic homolog of stomatin. (Stomatin is a major integral-membrane protein of mammalian erythrocytes.) Such NfeD/stomatin homolog gene pairs are present in more than 290 bacterial and archaeal genomes, and their protein products may be part of the machinery used for quality control of membrane proteins. Herein, we report the structure of the isolated C-terminal domain of PH0471, a Pyrococcus horikoshii NfeD homolog, which lacks the ClpP domain. This C-terminal domain (termed NfeDC) contains a five-strand beta-barrel, which is structurally very similar to the OB-fold (oligosaccharide/oligonucleotide-binding fold) domain. However, there is little sequence similarity between it and previously characterized OB-fold domains. The NfeDC domain lacks the conserved surface residues that are necessary for the binding of an OB-fold domain to DNA/RNA, an ion. Instead, its surface is composed of residues that are uniquely conserved in NfeD homologs and that form the structurally conserved surface turns and beta-bulges. There is also a conserved tryptophan present on the surface. We propose that, in general, NfeDC domains may interact with other spatially proximal membrane proteins and thereby regulate their activities. PubMed: 18687870DOI: 10.1110/ps.034736.108 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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