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Phosphorylation of spore coat proteins by a family of atypical protein kinases

Phosphorylation of spore coat proteins by a family of atypical protein kinasesThe modification of proteins by phosphorylation occurs in all life forms and is catalyzed by a large superfamily of enzymes known as protein kinases. We recently discovered a family of secretory pathway kinases that phosphorylate extracellular proteins. One member, family with sequence similarity 20C (Fam20C), is the physiological Golgi casein kinase. While examining distantly related protein sequences, we observed low levels of identity between the spore coat protein H (CotH), and the Fam20C-related secretory pathway kinases. CotH is a component of the spore in many bacterial and eukaryotic species, and is required for efficient germination of spores in Bacillus subtilis; however, the mechanism by which CotH affects germination is unclear. Here, we show that CotH is a protein kinase. The crystal structure of CotH reveals an atypical protein kinase-like fold with a unique mode of ATP binding. Examination of the genes neighboring cotH in B. subtilis led us to identify two spore coat proteins, CotB and CotG, as CotH substrates. Furthermore, we show that CotH-dependent phosphorylation of CotB and CotG is required for the efficient germination of B. subtilis spores. Collectively, our results define a family of atypical protein kinases and reveal an unexpected role for protein phosphorylation in spore biology.

Proc Natl Acad Sci U S A. 2016 Jun 21;113(25):E3482-91.
doi: 10.1073/pnas.1605917113.
Epub 2016 May 16.

PNAS Online

© 2016 National Academy of Sciences.

  Nguyen KB, Sreelatha A, Durrant ES, Lopez-Garrido J, Muszewska A, Dudkiewicz M, Grynberg M, Yee S, Pogliano K, Tomchick DR, Pawłowski K, Dixon JE, Tagliabracci VS.

Another SBC Highlight:

Crystal Structure of the FERM-SH2 Module of Human Jak2
Crystal Structure of the FERM-SH2 Module of Human Jak2.

Jak-family tyrosine kinases mediate signaling from diverse cytokine receptors. Binding of Jaks to their cognate receptors is mediated by their N-terminal region, which contains FERM and SH2 domains. Here we describe the crystal structure of the FERM-SH2 region of Jak2 at 3.0Å resolution.

 

PLoS One. 2016 May 26;11(5):e0156218. doi: 10.1371/journal.pone.0156218.
eCollection 2016.

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SBC Announcements:

 

19-ID Pilatus Detector

SBC is pleased to announce the introduction of a Pilatus 3 X 6M detector into the User Program at beamline 19-ID.
Data collected by our users has been of outstanding quality.

 

 

 

19-BM Rebotic sample mounter available

A robot is now available for use at beamline 19-BM. The sample dewar accommodates ten Unipuck magazines; pins must be 18mm in length and use either SSRL or ALS bases. Experienced users may now request remote access to 19-BM when applying for beamtime.

 

 

 

ALSO: Please Be Aware...!

 

APS requests the Experimental Safety Approval Form (ESAF) be submitted at least seven days prior to your scheduled beamtime.

 

Failure to submit your ESAF in advance may result in delaying the beginning of your experiment.

 

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Rapid Access Beamtime Available:

SBC Beamtime Request System

The on-line SBC Beamtime Request System allows users to view available beamtime on 19-ID and 19-BM, and to submit a request for rapid beamtime allocation.

Beamtime is available to the research community via a peer reviewed proposal system; it is supported by the U.S. Department of Energy, Office of Biological and Environmental Research.

Current Beamline Statistics:

APS PDB Depositions from BioSync
SBC Sector 19 2014 2015 2016 TOTAL
ID BM ID BM ID BM
PDB Depositions 263 36 235 30 80 13 4796

APS Publications Database:

Publications Total
SBC-CAT Publication List: 19-ID 1423
SBC-CAT Publication List: 19-BM 519
SBC-CAT Publication List: ALL
APS Publications Database

MCSG / APCF Announcements:

 

Beginning August 01, 2015 the Midwest Center for Structural Genomics (MCSG) will start accepting applications for access to the MCSG User Resource.

 

MCSG's structure determination platform is well established, and combines technologies, robotics and expertise for gene cloning, protein production, and crystallization, as well as biochemical and biophysical characterization.

 

For further information, please contact Andrzej Joachimiak.

 

Future Meetings:

 

12th International Conference on Biology and Synchrotron Radiation

August 21-24, 2016

SLAC National Accelerator Laboratory; Menlo Park, CA

 

X-Ray Methods in Structural Biology

October 10-25, 2016

Cold Spring Harbor Laboratory; Cold Spring Harbor, NY

 

De-Mystifying X-ray Data Processing in Macromolecular Crystallography

November 14-15, 2016

Charles Darwin House; London, UK

 

SBC Beamline Phone Numbers:

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19-ID Beamline Control Station 630-252-9823
19-ID Beamline Cordless Phone 630-252-0569
19-ID Beamline Inside D-Hutch 630-252-1819
 
19-BM Beamline Control Station 630-252-9833
19-BM Beamline Cordless Phone 630-252-0568
19-BM Beamline Inside D-Hutch 630-252-1719