1t6d: Difference between revisions

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[[Image:1t6d.jpg|left|200px]]
{{Seed}}
[[Image:1t6d.png|left|200px]]


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{{STRUCTURE_1t6d|  PDB=1t6d  |  SCENE=  }}  
{{STRUCTURE_1t6d|  PDB=1t6d  |  SCENE=  }}  


'''MIRAS phasing of the Aquifex aeolicus Ppx/GppA phosphatase: crystal structure of the type II variant'''
===MIRAS phasing of the Aquifex aeolicus Ppx/GppA phosphatase: crystal structure of the type II variant===




==Overview==
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Exopolyphosphatase/guanosine pentaphosphate phosphohydrolase (PPX/GPPA) enzymes play central roles in the bacterial stringent response induced by starvation. The high-resolution crystal structure of the putative Aquifex aeolicus PPX/GPPA phosphatase from the actin-like ATPase domain superfamily has been determined, providing the first insights to features of the common catalytic core of the PPX/GPPA family. The protein has a two-domain structure with an active site located in the interdomain cleft. Two crystal forms were investigated (type I and II) at resolutions of 1.53 and 2.15 A, respectively. This revealed a structural flexibility that has previously been described as a "butterfly-like" cleft opening around the active site in other actin-like superfamily proteins. A calcium ion is observed at the center of this region in type I crystals, substantiating that PPX/GPPA enzymes use metal ions for catalysis. Structural analysis suggests that nucleotides bind at a similar position to that seen in other members of the superfamily.
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{{ABSTRACT_PUBMED_15248747}}


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Structural characterization of the stringent response related exopolyphosphatase/guanosine pentaphosphate phosphohydrolase protein family., Kristensen O, Laurberg M, Liljas A, Kastrup JS, Gajhede M, Biochemistry. 2004 Jul 20;43(28):8894-900. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15248747 15248747]
Structural characterization of the stringent response related exopolyphosphatase/guanosine pentaphosphate phosphohydrolase protein family., Kristensen O, Laurberg M, Liljas A, Kastrup JS, Gajhede M, Biochemistry. 2004 Jul 20;43(28):8894-900. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15248747 15248747]
Role of inorganic polyphosphate in promoting ribosomal protein degradation by the Lon protease in E. coli., Kuroda A, Nomura K, Ohtomo R, Kato J, Ikeda T, Takiguchi N, Ohtake H, Kornberg A, Science. 2001 Jul 27;293(5530):705-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11474114 11474114]
Guanosine pentaphosphate phosphohydrolase of Escherichia coli is a long-chain exopolyphosphatase., Keasling JD, Bertsch L, Kornberg A, Proc Natl Acad Sci U S A. 1993 Aug 1;90(15):7029-33. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8394006 8394006]
Exopolyphosphate phosphatase and guanosine pentaphosphate phosphatase belong to the sugar kinase/actin/hsp 70 superfamily., Reizer J, Reizer A, Saier MH Jr, Bork P, Sander C, Trends Biochem Sci. 1993 Jul;18(7):247-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8212131 8212131]
[[Category: Aquifex aeolicus vf5]]
[[Category: Aquifex aeolicus vf5]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Actin-like fold]]
[[Category: Actin-like fold]]
[[Category: Alpha/beta protein]]
[[Category: Alpha/beta protein]]
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