2GEM

2.1A crystal structure of Salmonella tyhpimurium YeaZ, a putative Gram-negative RPF, form-A

Summary for 2GEM

• Entry DOI: 10.2210/pdb2gem/pdb
• Related: 2GEL
• Descriptor: Putative Gram negative resuscitation promoting factor (2 entities in total)
• Functional Keywords: m22, glycoprotease, yeaz, actin-like-fold, chaperone
• Biological source: Salmonella typhimurium
• Cellular location: Cytoplasm : Q7CQE0
• Total number of polymer chains: 2
• Total formula weight: 49532.34

Authors

Nichols, C.E.,Stammers, D.K. (deposition date: 2006-03-20, release date: 2006-08-01, Last modification date: 2024-11-20)

Primary citation

Nichols, C.E.,Johnson, C.,Lockyer, M.,Charles, I.G.,Lamb, H.K.,Hawkins, A.R.,Stammers, D.K.
Structural Characterization of Salmonella typhimurium YeaZ, an M22 O-Sialoglycoprotein Endopeptidase Homolog
Proteins, 64:111-123, 2006

PubMed Abstract: The Salmonella typhimurium "yeaZ" gene (StyeaZ) encodes an essential protein of unknown function (StYeaZ), which has previously been annotated as a putative homolog of the Pasteurella haemolytica M22 O-sialoglycoprotein endopeptidase Gcp. YeaZ has also recently been reported as the first example of an RPF from a gram-negative bacterial species. To further characterize the properties of StYeaZ and the widely occurring MK-M22 family, we describe the purification, biochemical analysis, crystallization, and structure determination of StYeaZ. The crystal structure of StYeaZ reveals a classic two-lobed actin-like fold with structural features consistent with nucleotide binding. However, microcalorimetry experiments indicated that StYeaZ neither binds polyphosphates nor a wide range of nucleotides. Additionally, biochemical assays show that YeaZ is not an active O-sialoglycoprotein endopeptidase, consistent with the lack of the critical zinc binding motif. We present a detailed comparison of YeaZ with available structural homologs, the first reported structural analysis of an MK-M22 family member. The analysis indicates that StYeaZ has an unusual orientation of the A and B lobes which may require substantial relative movement or interaction with a partner protein in order to bind ligands. Comparison of the fold of YeaZ with that of a known RPF domain from a gram-positive species shows significant structural differences and therefore potentially distinctive RPF mechanisms for these two bacterial classes.

PubMed: 16617437
DOI: 10.1002/prot.20982

Experimental method

X-RAY DIFFRACTION (2.1 Å)