1ye8: Difference between revisions

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[[Image:1ye8.gif|left|200px]]
{{Seed}}
[[Image:1ye8.png|left|200px]]


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{{STRUCTURE_1ye8|  PDB=1ye8  |  SCENE=  }}  
{{STRUCTURE_1ye8|  PDB=1ye8  |  SCENE=  }}  


'''Crystal Structure of THEP1 from the hyperthermophile Aquifex aeolicus'''
===Crystal Structure of THEP1 from the hyperthermophile Aquifex aeolicus===




==Overview==
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BACKGROUND: aaTHEP1, the gene product of aq_1292 from Aquifex aeolicus, shows sequence homology to proteins from most thermophiles, hyperthermophiles, and higher organisms such as man, mouse, and fly. In contrast, there are almost no homologous proteins in mesophilic unicellular microorganisms. aaTHEP1 is a thermophilic enzyme exhibiting both ATPase and GTPase activity in vitro. Although annotated as a nucleotide kinase, such an activity could not be confirmed for aaTHEP1 experimentally and the in vivo function of aaTHEP1 is still unknown. RESULTS: Here we report the crystal structure of selenomethionine substituted nucleotide-free aaTHEP1 at 1.4 A resolution using a multiple anomalous dispersion phasing protocol. The protein is composed of a single domain that belongs to the family of 3-layer (alpha/beta/alpha)-structures consisting of nine central strands flanked by six helices. The closest structural homologue as determined by DALI is the RecA family. In contrast to the latter proteins, aaTHEP1 possesses an extension of the beta-sheet consisting of four additional beta-strands. CONCLUSION: We conclude that the structure of aaTHEP1 represents a variation of the RecA fold. Although the catalytic function of aaTHEP1 remains unclear, structural details indicate that it does not belong to the group of GTPases, kinases or adenosyltransferases. A mainly positive electrostatic surface indicates that aaTHEP1 might be a DNA/RNA modifying enzyme. The resolved structure of aaTHEP1 can serve as paradigm for the complete THEP1 family.
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{{ABSTRACT_PUBMED_15777481}}


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Crystal structure of THEP1 from the hyperthermophile Aquifex aeolicus: a variation of the RecA fold., Rossbach M, Daumke O, Klinger C, Wittinghofer A, Kaufmann M, BMC Struct Biol. 2005 Mar 20;5:7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15777481 15777481]
Crystal structure of THEP1 from the hyperthermophile Aquifex aeolicus: a variation of the RecA fold., Rossbach M, Daumke O, Klinger C, Wittinghofer A, Kaufmann M, BMC Struct Biol. 2005 Mar 20;5:7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15777481 15777481]
Glycosaminoglycans in human retinoblastoma cells: heparan sulfate, a modulator of the pigment epithelium-derived factor-receptor interactions., Alberdi EM, Weldon JE, Becerra SP, BMC Biochem. 2003 Feb 19;4:1. Epub 2003 Feb 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12625842 12625842]
[[Category: Aquifex aeolicus]]
[[Category: Aquifex aeolicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Mixed alpha-beta protein]]
[[Category: Mixed alpha-beta protein]]
[[Category: Rossman fold]]
[[Category: Rossman fold]]
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