Portal de Periódicos da CAPES

Structure of the hypothetical protein AQ_1354 from Aquifex aeolicus

2003; Wiley; Volume: 59; Issue: 7 Linguagem: Inglês

10.1107/s0907444903011028

1399-0047

Vaheh Oganesyan, Didier Busso, Jeroen Brandsen, Shengfeng Chen, Jaru Jancarik, Rosalind Kim, Sung‐Hou Kim,

Protein Structure and Dynamics

The crystal structure of a hypothetical protein AQ_1354 (gi 2983779) from the hyperthermophilic bacteria Aquifex aeolicus has been determined using X-ray crystallography. As found in many structural genomics studies, this protein is not associated with any known function based on its amino-acid sequence. PSI-BLAST analysis against a non-redundant sequence database gave 68 similar sequences referred to as `conserved hypothetical proteins' from the uncharacterized protein family UPF0054 (accession No. PF02310). Crystallographic analysis revealed that the overall fold of this protein consists of one central α-helix surrounded by a four-stranded β-sheet and four other α-helices. Structure-based homology analysis with DALI revealed that the structure has a moderate to good resemblance to metal-dependent proteinases such as collagenases and gelatinases, thus suggesting its possible molecular function. However, experimental tests for collagen­ase and gelatinase-type function show no detectable activity under standard assay conditions. Therefore, we suggest either that the members of the UPF0054 family have a similar fold but different biochemical functions to those of collagenases and gelatinases or that they have a similar function but perform it under different conditions.