Structural Characterization of Salmonella typhimurium Yeaz, an M22 O-Sialoglycoprotein Endopeptidase Homolog

Nichols, C; Johnson, C; Lockyer, M; Charles, IG; Lamb, H; Hawkins, A; Stammers, D

Structural Characterization of Salmonella typhimurium Yeaz, an M22 O-Sialoglycoprotein Endopeptidase Homolog

Nichols, C Johnson, C Lockyer, M Charles, IG Lamb, H Hawkins, A Stammers, D

Permalink

Publisher:: Wiley-Liss
Publication Type:: Journal Article
Citation:: Proteins-Structure Function And Bioinformatics, 2006, 64 (1), pp. 111 - 123
Issue Date:: 2006-01

Closed Access

	Filename	Description	Size
	2009002955OK.pdf		2.7 MB	Adobe PDF	View/Open

Copyright Clearance Process

Recently Added
In Progress
Closed Access

This item is closed access and not available.

Full metadata record

Field	Value	Language
dc.contributor.author	Nichols, C	en_US
dc.contributor.author	Johnson, C	en_US
dc.contributor.author	Lockyer, M	en_US
dc.contributor.author	Charles, IG	en_US
dc.contributor.author	Lamb, H	en_US
dc.contributor.author	Hawkins, A	en_US
dc.contributor.author	Stammers, D	en_US
dc.date.issued	2006-01	en_US
dc.identifier.citation	Proteins-Structure Function And Bioinformatics, 2006, 64 (1), pp. 111 - 123	en_US
dc.identifier.issn	0887-3585	en_US
dc.identifier.uri	http://hdl.handle.net/10453/13266
dc.description.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 Gep. 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.	en_US
dc.publisher	Wiley-Liss	en_US
dc.relation.ispartof	Proteins-Structure Function And Bioinformatics	en_US
dc.relation.isbasedon	10.1002/prot.20982	en_US
dc.subject.classification	Bioinformatics	en_US
dc.title	Structural Characterization of Salmonella typhimurium Yeaz, an M22 O-Sialoglycoprotein Endopeptidase Homolog	en_US
dc.type	Journal Article
utslib.citation.volume	1	en_US
utslib.citation.volume	64	en_US
utslib.location.activity	ISI:000237935800012	en_US
utslib.for	0707 Veterinary Sciences	en_US
utslib.for	01 Mathematical Sciences	en_US
utslib.for	06 Biological Sciences	en_US
utslib.for	08 Information and Computing Sciences	en_US
dc.location.activity	ISI:000237935800012	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Engineering and Information Technology
pubs.organisational-group	/University of Technology Sydney/Faculty of Engineering and Information Technology/School of Electrical and Data Engineering
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Strength - ithree - Institute of Infection, Immunity and Innovation
utslib.copyright.status	closed_access
pubs.consider-herdc	false	en_US
pubs.issue	1	en_US
pubs.volume	64	en_US

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 Gep. 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.

Please use this identifier to cite or link to this item:

http://hdl.handle.net/10453/13266