1OZ9

Crystal structure of AQ_1354, a hypothetical protein from Aquifex aeolicus

Summary for 1OZ9

• Entry DOI: 10.2210/pdb1oz9/pdb
• Descriptor: Hypothetical protein AQ_1354 (2 entities in total)
• Functional Keywords: matrix metalloproteinase type fold, structural genomics, bsgc structure funded by nih, protein structure initiative, psi, berkeley structural genomics center, unknown function
• Biological source: Aquifex aeolicus
• Cellular location: Cytoplasm (By similarity): O67367
• Total number of polymer chains: 1
• Total formula weight: 17372.02

Authors

Oganesyan, V.,Busso, D.,Brandsen, J.,Chen, S.,Jancarik, J.,Kim, R.,Kim, S.H.,Berkeley Structural Genomics Center (BSGC) (deposition date: 2003-04-08, release date: 2003-09-23, Last modification date: 2024-02-14)

Primary citation

Oganesyan, V.,Busso, D.,Brandsen, J.,Chen, S.,Jancarik, J.,Kim, R.,Kim, S.H.
Structure of the hypothetical protein AQ_1354 from Aquifex aeolicus.
Acta Crystallogr.,Sect.D, 59:1219-1223, 2003

PubMed Abstract: 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 alpha-helix surrounded by a four-stranded beta-sheet and four other alpha-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.

PubMed: 12832766
DOI: 10.1107/S0907444903011028

Experimental method

X-RAY DIFFRACTION (1.894 Å)