1LFP

Crystal Structure of a Conserved Hypothetical Protein Aq1575 from Aquifex Aeolicus

Summary for 1LFP

• Entry DOI: 10.2210/pdb1lfp/pdb
• Descriptor: Hypothetical protein AQ_1575 (2 entities in total)
• Functional Keywords: hypothetical, new fold, thermostability, structural genomics, bsgc structure funded by nih, protein structure initiative, psi, berkeley structural genomics center, rna binding protein
• Biological source: Aquifex aeolicus
• Total number of polymer chains: 1
• Total formula weight: 28040.40

Authors

Shin, D.H.,Yokota, H.,Kim, R.,Kim, S.H.,Berkeley Structural Genomics Center (BSGC) (deposition date: 2002-04-11, release date: 2002-06-19, Last modification date: 2024-11-06)

Primary citation

Shin, D.H.,Yokota, H.,Kim, R.,Kim, S.H.
Crystal structure of conserved hypothetical protein Aq1575 from Aquifex aeolicus.
Proc.Natl.Acad.Sci.USA, 99:7980-7985, 2002

PubMed Abstract: The crystal structure of a conserved hypothetical protein, Aq1575, from Aquifex aeolicus has been determined by using x-ray crystallography. The protein belongs to the domain of unknown function DUF28 in the Pfam and PALI databases for which there was no structural information available until now. A structural homology search with the DALI algorithm indicates that this protein has a new fold with no obvious similarity to those of other proteins of known three-dimensional structure. The protein reveals a monomer consisting of three domains arranged along a pseudo threefold symmetry axis. There is a large cleft with approximate dimensions of 10 A x 10 A x 20 A in the center of the three domains along the symmetry axis. Two possible active sites are suggested based on the structure and multiple sequence alignment. There are several highly conserved residues in these putative active sites. The structure based molecular properties and thermostability of the protein are discussed.

PubMed: 12060744
DOI: 10.1073/pnas.132241399

Experimental method

X-RAY DIFFRACTION (1.72 Å)