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2005年07月15日

【期刊论文】Crystal structure of the YML079w protein from Saccharomyces cerevisiae reveals a new sequence family of the jelly-roll fold

周丛照， CONG-ZHAO ZHOU，， PHILIPPE MEYER， SOPHIE QUEVILLON-CHERUEL， IN

Protein Science (2005), 14: 209-215. Published by Cold Spring Harbor Laboratory Press. Copyright，-0001，（）：

-1年11月30日

摘要

We determined the three-dimensional crystal structure of the protein YML079wp, encoded by a hypothetical open reading frame from Saccharomyces cerevisiae to a resolution of 1.75

jelly-roll motif， cupin superfamily， structural genomics， YML079wp， S.， cerevisiae

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2005年07月15日

【期刊论文】Crystal Structure of the Yeast Phox Homology (PX) Domain Protein Grd19p Complexed to Phosphatidylinositol-3-phosphate*

周丛照， Cong-Zhao Zhou‡， Ines Li de La Sierra-Gallay§， Sophie Quevillon-Cheruel‡， Bruno Collinet‡， Philippe Minard‡， Karine Blondeau¶， Gilles Henckes¶， Robert Aufrere¶， Nicolas Leulliot‡， Marc Graille§， Isabelle Sorel‡， Philippe Savarin§， Francoise de la Torre§， Anne Poupon§， Joel Janin§， and Hermanvan Tilbeurgh‡

THE JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278(50)50371-50376，-0001，（）：

-1年11月30日

摘要

Phox homology (PX) domains have been recently identified in a number of different proteins and are involved in various cellular functions such as vacuolar targeting and membrane protein trafficking. It was shown that these modules of about 130 amino acids specifically binding to phosphoinositides and that this interaction is crucial for their cellular function. The yeast genome contains 17 PX domain proteins. One of these, Grd19p, is involved in the localization of the late Golgi membrane proteins DPAP A and Kex2p. Grd19p consists of the PX domain with 30 extra residues at the N-terminal and is homologous to the functionally characterized human sorting nexin protein SNX3. We determined the 2.0 Å crystal structure of Grd19p in the free form and in complex with D-myo-phosphatidylinositol 3-phosphate (diC4PtdIns (3) P), representing the first case of both free and ligand-bound conformations of the same PX module. The ligand occupies a well defined positively charged binding pocket at the interface between the β-sheet and α-helical parts of the molecule. The structure of the free and bound protein are globally similar but show some significant differences in aregion containing a polyproline peptide and a putative membrane attachmentsite.

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2005年07月15日

【期刊论文】Activation of the LicT Transcriptional Antiterminator Involves a Domain Swing⁄Lock Mechanism Provoking Massive Structural Changes*□

周丛照， Marc Graille‡§， Cong-Zhao Zhou§¶， Veronique Receveur-Brechot**， Bruno Collinet¶， Nathalie Declerck‡‡§§， and Herman van Tilbeurgh‡¶¶

THE JOURNAL OF BIOLOGICAL CHEMISTRY 280(15)14780-14789, 2005，-0001，（）：

-1年11月30日

摘要

The transcriptional antiterminator protein Lic Tregulates the expression of Bacillus subtilis operons involved in-glucoside metabolism. It consists of an Nterminal RNA-binding domain (co-antiterminator (CAT)) and two phosphorylatable phosphotransferase system regulation domains (PRD1 and PRD2). In the activated state, each PRD forms a dimericunit with the phosphorylation sites totally buried at the dimer interface. Here we present the 1.95

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周丛照邀请

中国科学技术大学，安徽

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