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2012
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PDB Deposits:
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15
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6
1505
 

actor robot available for use on 19ID9ID

Remote Data Collection on 19ID for experienced users

A fully motorized Mini-beam device for use on 19ID

•19BM upgraded and available for immediate beamtime  

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STUDY REVEALS HOW EBOLA BLOCKS IMMUNE SYSTEM

Image Krishna Kumar via Getty Images

 

APS/APCF Symposium & MCSG 14th Annual Meeting

The symposium reviewed the achievements of X-ray macromolecular crystallography and the future structural biology opportunities in biomedical and biological sciences. We assessed the progress on understanding structures of proteins and their families and will contemplate the future impact of new free electron laser light sources on biology and chemistry. The potential contribution and impact of Advanced Photon Source upgrade and new protein research facilities were discussed in the context of future advances in structural and molecular biology. Thank you to those who attended. 

The United Nations Educational, Scientific and Cultural Organization (UNESCO) and the International Union of Crystallography (IUCr) commemorates the centennial of X-ray diffraction and declares 2014 the International Year of Crystallography.

 

lessening x-ray damage is healthy for protein discovery data

 

Newly ID'd protein provides tArget for antibiotic-resistant hospital bacterium

 

Structural Biology Reveals the Secrets of Disease

 

 

 

 

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Gallary of Journal Covers

 

Safety Training The SBC is dedicated to performing scientific research in a safe and environmentally sound manner. No job or experiment at the SBC is given authorization to proceed without first performing a review of the hazards involved and the controls to be implemented regardless of beamtime scheduling and/or cost impacts.
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Ebola Virus VP24 Targets a Unique NLS Binding Site on Karyopherin Alpha 5 to Selectively Compete with Nuclear Import of Phosphorylated STAT1.

Xu W, Edwards MR, Borek DM, Feagins AR, Mittal A, Alinger JB, Berry KN, Yen B, Hamilton J, Brett TJ, Pappu RV, Leung DW, Basler CF, Amarasinghe GK. Cell Host Microbe. 2014 Aug 13;16(2):187-200.

Representative 1:1 complex structure between eVP24/KPNA5C reveals multiple structural interaction elements between the two molecules.

 

During antiviral defense, interferon (IFN) signaling triggers nuclear transport of tyrosine-phosphorylated STAT1 (PY-STAT1), which occurs via a subset of karyopherin alpha (KPNA) nuclear transporters. Many viruses, including Ebola virus, actively antagonize STAT1 signaling to counteract the antiviral effects of IFN. Ebola virus VP24 protein (eVP24) binds KPNA to inhibit PY-STAT1 nuclear transport and render cells refractory to IFNs. We describe the structure of human KPNA5 C terminus in complex with eVP24. In the complex, eVP24 recognizes a unique nonclassical nuclear localization signal (NLS) binding site on KPNA5 that is necessary for efficient PY-STAT1 nuclear transport. eVP24 binds KPNA5 with very high affinity to effectively compete with and inhibit PY-STAT1 nuclear transport. In contrast, eVP24 binding does not affect the transport of classical NLS cargo. Thus, eVP24 counters cell-intrinsic innate immunity by selectively targeting PY-STAT1 nuclear import while leaving the transport of other cargo that may be required for viral replication unaffected.

PDB: 4U2X

>> see related article

 

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