3D local structure around Zn in Kti11p as a representative Zn-(Cys)4 motif as obtained by MXAN.
Zinc is an important component of many proteins that play key roles in transcription, translation, and catalysis. Kti11p, DESR1, both belonging to a protein family characterized by a CSL zinc finger domain, and the co-catalytic zinc-protein PML containing a Zn(2+) binding domain called RING or C(3)HC(4) finger are all structurally determined by NMR although the zinc sites are silent to this spectroscopical method. The comparison of X-ray absorption near-edge spectroscopy (XANES) data for the three proteins demonstrates that fingerprints effect is a reliable method for a primary characterization of ligand species. Ab initio full MS calculations performed by MXAN are applied to obtain chemical and stereo structural information around the Zn ion in Kti11p. For the first time this high-spatial resolution technique confirms the formation of a stable Zn tetrahedral configuration with four sulfur ligands, and returns extremely accurate bond angle information between ligands.
Yu
Meijuan
M
Institute of High Energy Physics, Chinese Academy of Sciences, Beijing Synchrotron Radiation Facility, 19B YuquanLu, Shijingshan District, Beijing 100049, China.
Yang
Feifei
F
Chu
Wangsheng
W
Wang
Yu
Y
Zhao
Haifeng
H
Gao
Bin
B
Zhao
Wei
W
Sun
Jianping
J
Wu
Fangming
F
Zhang
Xiaowei
X
Shi
Yunyu
Y
Wu
Ziyu
Z
D000042:Absorption; D020816:Amino Acid Motifs; D003545:Cysteine / Q000737:chemistry*; D011487:Protein Conformation; D012097:Repressor Proteins / Q000737:chemistry*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*; D013057:Spectrum Analysis / Q000379:methods; D014965:X-Rays; D015032:Zinc / Q000737:chemistry*
C459979:KTI11 protein, S cerevisiae; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; D015032:Zinc; D003545:Cysteine