8K8L

Structure of Klebsiella pneumonia ModA with molybdate

Summary for 8K8L

• Entry DOI: 10.2210/pdb8k8l/pdb
• Descriptor: Molybdate transporter periplasmic protein, MOLYBDATE ION (3 entities in total)
• Functional Keywords: molybdate binding protein, metal binding protein
• Biological source: Klebsiella pneumoniae subsp. pneumoniae (strain HS11286)
• Total number of polymer chains: 1
• Total formula weight: 27168.70

Authors

Zhao, Q.,Bartlam, M. (deposition date: 2023-07-31, release date: 2023-11-01)

Primary citation

Zhao, Q.,Su, X.,Wang, Y.,Liu, R.,Bartlam, M.
Structural analysis of molybdate binding protein ModA from Klebsiella pneumoniae.
Biochem.Biophys.Res.Commun., 681:41-46, 2023

PubMed Abstract: Klebsiella pneumoniae, a facultative anaerobe, relies on acquiring molybdenum to sustain growth in anaerobic conditions, a crucial factor for the pathogen to establish infections within host environments. Molybdenum plays a critical role in pathogenesis as it forms an essential component of cofactors for molybdoenzymes. K. pneumoniae utilizes the ABC (ATP-Binding-Cassette) transporter encoded by the modABC operon for uptake of the group VI elements molybdenum and tungsten. In this study, we determined the X-ray crystal structures of both the molybdenum-free and molybdenum-bound substrate-binding protein (SBP) ModA from Klebsiella pneumoniae to 2.00 Å and 1.77 Å resolution respectively. ModA crystallizes in the space group P222 with a single monomer in one asymmetric unit. The purified protein remained soluble and specifically bound molybdate and tungstate with K values of 6.3 nM and 5.2 nM, respectively. Tungstate competes with molybdate by binding to ModA, resulting in enhanced antimicrobial activity. These data provide a starting point for structural and functional analyses of molybdate transport in K. pneumoniae.

PubMed: 37751633
DOI: 10.1016/j.bbrc.2023.09.055

Experimental method

X-RAY DIFFRACTION (1.77 Å)