1ye8: Difference between revisions

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[[Image:1ye8.gif|left|200px]]<br /><applet load="1ye8" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1ye8.gif|left|200px]]<br /><applet load="1ye8" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1ye8, resolution 1.40Å" />

'''Crystal Structure of THEP1 from the hyperthermophile Aquifex aeolicus'''<br />

==Overview==

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.

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.

==About this Structure==

1YE8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] with MG, NA and PO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1YE8 OCA].

1YE8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YE8 OCA].

==Reference==

Line 23:

[[Category: mixed alpha-beta protein; rossman fold]]

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@@ Line 1: / Line 1: @@
-[[Image:1ye8.gif|left|200px]]<br /><applet load="1ye8" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1ye8.gif|left|200px]]<br /><applet load="1ye8" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1ye8, resolution 1.40&Aring;" />
 '''Crystal Structure of THEP1 from the hyperthermophile Aquifex aeolicus'''<br />
 ==Overview==
-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.
+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.
 ==About this Structure==
-YE8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] with MG, NA and PO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YE8 OCA].
+YE8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YE8 OCA].
 ==Reference==
@@ Line 23: / Line 23: @@
 [[Category: mixed alpha-beta protein; rossman fold]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:42:50 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:04:23 2008''