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Structure and function of human Naa60 (NatF), a Golgi-localized bi-functional acetyltransferase

Phosphorylation of spore coat proteins by a family of atypical protein kinasesN-terminal acetylation (Nt-acetylation), carried out by N-terminal acetyltransferases (NATs), is a conserved and primary modification of nascent peptide chains. Naa60 (also named NatF) is a recently identified NAT found only in multicellular eukaryotes. This protein was shown to locate on the Golgi apparatus and mainly catalyze the Nt-acetylation of transmembrane proteins, and it also harbors lysine Nε-acetyltransferase (KAT) activity to catalyze the acetylation of lysine ε-amine. Here, we report the crystal structures of human Naa60 (hNaa60) in complex with Acetyl-Coenzyme A (Ac-CoA) or Coenzyme A (CoA). The hNaa60 protein contains an amphipathic helix following its GNAT domain that may contribute to Golgi localization of hNaa60, and the β7-β8 hairpin adopted different conformations in the hNaa60(1-242) and hNaa60(1-199) crystal structures. Remarkably, we found that the side-chain of Phe 34 can influence the position of the coenzyme, indicating a new regulatory mechanism involving enzyme, co-factor and substrates interactions. Moreover, structural comparison and biochemical studies indicated that Tyr 97 and His 138 are key residues for catalytic reaction and that a non-conserved β3-β4 long loop participates in the regulation of hNaa60 activity.

Sci Rep. 2016 Aug 23;6:31425.
doi: 10.1038/srep31425.

© 2016 Macmillan Publishers Limited, part of Springer Nature.

  Chen JY, Liu L, Cao CL, Li MJ, Tan K, Yang X, Yun CH.

Another SBC Highlight:

Bile salt receptor complex activates a pathogenic type III secretion system
Bile salt receptor complex activates a pathogenic type III secretion system.


Bile is an important component of the human gastrointestinal tract with an essential role in food absorption and antimicrobial activities. Enteric bacterial pathogens have developed strategies to sense bile as an environmental cue to regulate virulence genes during infection.



Elife. 2016 Jul 5;5. pii: e15718.
doi: 10.7554/eLife.15718.

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19-ID Pilatus Detector


SBC has implemented 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 Robotic 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.



SBC Staff Hosting Changes


SBC staff are now available for User Support between the hours of 8:00am and 10:pm.




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
PDB Depositions 263 36 252 30 103 17 4840

APS Publications Database:

Publications Total
SBC-CAT Publication List: 19-ID 1435
SBC-CAT Publication List: 19-BM 520
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:


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


DLS-CCP4 Data Collection and Structure Solution Workshop

December 13-20, 2016

Diamond Light Source; Oxfordshire, UK


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