2KPP

Solution NMR structure of Lin0431 protein from Listeria innocua. Northeast Structural Genomics Consortium Target LkR112

Summary for 2KPP

• Entry DOI: 10.2210/pdb2kpp/pdb
• NMR Information: BMRB: 16563
• Descriptor: Lin0431 protein (1 entity in total)
• Functional Keywords: solution nmr structure, structural genomics, psi-2, protein structure initiative, northeast structural genomics consortium, nesg, unknown function
• Biological source: Listeria innocua
• Total number of polymer chains: 1
• Total formula weight: 12808.54

Authors

Tang, Y.,Xiao, R.,Ciccosanti, C.,Janjua, H.,Lee, D.Y.,Everett, J.K.,Swapna, G.V.T.,Acton, T.B.,Rost, B.,Montelione, G.T.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2009-10-18, release date: 2010-02-23, Last modification date: 2024-05-08)

Primary citation

Tang, Y.,Xiao, R.,Ciccosanti, C.,Janjua, H.,Lee, D.Y.,Everett, J.K.,Swapna, G.V.,Acton, T.B.,Rost, B.,Montelione, G.T.
Solution NMR structure of Lin0431 protein from Listeria innocua reveals high structural similarity with domain II of bacterial transcription antitermination protein NusG.
Proteins, 78:2563-2568, 2010

PubMed Abstract: Lin0431 protein from (UniProtKB/TrEMBL ID Q92EM7/Q92EM7_LISIN) was selected as a target of the Northeast Structural Genomics Consortium (target ID: LkR112). Here, we present the high-quality NMR solution structure of this protein which is the first representative for a member of DUF1312 domain family. Lin0431 protein exhibits a β-sandwich topology. Four anti-parallel β-strands form one face of the sandwich and the other three anti-parallel β-strands together with a short α-helix form the other face of the sandwich. Structure alignment by Dali reveals an unexpected structural similarity with domain II of NusG from . Analyses of the electrostatic protein surface potential and searches for protein surface cavities reveal the conserved basic charged surface cavities of both the Lin0431 and domain II of NusG, suggesting they may bind the negatively charged nucleic acids and/or and other binding partners. The high structural similarity and similar surface features, despite the lack of recognizable sequence similarity, between Lin0431 and NusG domain II suggest that the domain II of NusG and DUF1312 domains have a homologous relationship and may share similar biochemical functions.

PubMed: 20602357
DOI: 10.1002/prot.22760

Experimental method

SOLUTION NMR