1huf: Difference between revisions
New page: left|200px<br /><applet load="1huf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1huf, resolution 2.0Å" /> '''CRYSTAL STRUCTURE OF ... |
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'''CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF THE TYROSINE PHOSPHATASE YOPH FROM YERSINIA PESTIS.'''<br /> | '''CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF THE TYROSINE PHOSPHATASE YOPH FROM YERSINIA PESTIS.'''<br /> | ||
==Overview== | ==Overview== | ||
Yersinia pestis, the causative agent of bubonic plague, injects effector | Yersinia pestis, the causative agent of bubonic plague, injects effector proteins into the cytosol of mammalian cells that enable the bacterium to evade the immune response of the infected organism by interfering with eukaryotic signal transduction pathways. YopH is a modular effector composed of a C-terminal protein tyrosine phosphatase (PTPase) domain and a multifunctional N-terminal domain that not only orchestrates the secretion and translocation of YopH into eukaryotic cells but also binds tyrosine-phosphorylated target proteins to mediate substrate recognition. The crystal structure of the N-terminal domain of YopH (YopH(N); residues 1-130) has been determined at 2.0 A resolution. The amino-acid sequences that target YopH for secretion from the bacterium and translocation into eukaryotic cells form integral parts of this compactly folded domain. The structure of YopH(N) bears no resemblance to eukaryotic phosphotyrosine-binding domains, nor is it reminiscent of any known fold. Residues that have been implicated in phosphotyrosine-dependent protein binding are clustered together on one face of YopH(N), but the structure does not suggest a mechanism for protein-phosphotyrosine recognition. | ||
==About this Structure== | ==About this Structure== | ||
1HUF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Active as [http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] Full crystallographic information is available from [http:// | 1HUF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Active as [http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HUF OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Yersinia pestis]] | [[Category: Yersinia pestis]] | ||
[[Category: Evdokimov, A | [[Category: Evdokimov, A G.]] | ||
[[Category: Waugh, D | [[Category: Waugh, D S.]] | ||
[[Category: beta hairpin]] | [[Category: beta hairpin]] | ||
[[Category: helical bundle]] | [[Category: helical bundle]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:04:58 2008'' | ||
Revision as of 14:05, 21 February 2008
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CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF THE TYROSINE PHOSPHATASE YOPH FROM YERSINIA PESTIS.
OverviewOverview
Yersinia pestis, the causative agent of bubonic plague, injects effector proteins into the cytosol of mammalian cells that enable the bacterium to evade the immune response of the infected organism by interfering with eukaryotic signal transduction pathways. YopH is a modular effector composed of a C-terminal protein tyrosine phosphatase (PTPase) domain and a multifunctional N-terminal domain that not only orchestrates the secretion and translocation of YopH into eukaryotic cells but also binds tyrosine-phosphorylated target proteins to mediate substrate recognition. The crystal structure of the N-terminal domain of YopH (YopH(N); residues 1-130) has been determined at 2.0 A resolution. The amino-acid sequences that target YopH for secretion from the bacterium and translocation into eukaryotic cells form integral parts of this compactly folded domain. The structure of YopH(N) bears no resemblance to eukaryotic phosphotyrosine-binding domains, nor is it reminiscent of any known fold. Residues that have been implicated in phosphotyrosine-dependent protein binding are clustered together on one face of YopH(N), but the structure does not suggest a mechanism for protein-phosphotyrosine recognition.
About this StructureAbout this Structure
1HUF is a Single protein structure of sequence from Yersinia pestis. Active as Protein-tyrosine-phosphatase, with EC number 3.1.3.48 Full crystallographic information is available from OCA.
ReferenceReference
Structure of the N-terminal domain of Yersinia pestis YopH at 2.0 A resolution., Evdokimov AG, Tropea JE, Routzahn KM, Copeland TD, Waugh DS, Acta Crystallogr D Biol Crystallogr. 2001 Jun;57(Pt 6):793-9. Epub 2001, May 25. PMID:11375498
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