2ZWR

Crystal structure of TTHA1623 from thermus thermophilus HB8

Summary for 2ZWR

• Entry DOI: 10.2210/pdb2zwr/pdb
• Descriptor: Metallo-beta-lactamase superfamily protein, ZINC ION (3 entities in total)
• Functional Keywords: metallo-beta-lactamase, hydrolase
• Biological source: Thermus thermophilus
• Total number of polymer chains: 2
• Total formula weight: 45559.02

Authors

Yamamura, A.,Okada, A.,Kameda, Y.,Ohtsuka, J.,Nakagawa, N.,Ebihara, A.,Yokoyama, S.,Kuramitsu, S.,Nagata, K.,Tanokura, M. (deposition date: 2008-12-17, release date: 2009-10-06, Last modification date: 2024-03-13)

Primary citation

Yamamura, A.,Okada, A.,Kameda, Y.,Ohtsuka, J.,Nakagawa, N.,Ebihara, A.,Nagata, K.,Tanokura, M.
Structure of TTHA1623, a novel metallo-beta-lactamase superfamily protein from Thermus thermophilus HB8
Acta Crystallogr.,Sect.F, 65:455-459, 2009

PubMed Abstract: TTHA1623 is a metallo-beta-lactamase superfamily protein from the extremely thermophilic bacterium Thermus thermophilus HB8. Homologues of TTHA1623 exist in a wide range of bacteria and archaea and one eukaryote, Giardia lamblia, but their function remains unknown. To analyze the structural properties of TTHA1623, the crystal structures of its iron-bound and zinc-bound forms have been determined to 2.8 and 2.2 A resolution, respectively. TTHA1623 possesses an alphabetabetaalpha-fold similar to that of other metallo-beta-lactamase superfamily proteins with glyoxalase II-type metal coordination. However, TTHA1623 exhibits a putative substrate-binding pocket with a unique shape.

PubMed: 19407375
DOI: 10.1107/S174430910901361X

Experimental method

X-RAY DIFFRACTION (2.2 Å)