1xqi: Difference between revisions
New page: left|200px<br /><applet load="1xqi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xqi, resolution 2.50Å" /> '''Crystal Structure An... |
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[[Image:1xqi.gif|left|200px]]<br /><applet load="1xqi" size=" | [[Image:1xqi.gif|left|200px]]<br /><applet load="1xqi" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1xqi, resolution 2.50Å" /> | caption="1xqi, resolution 2.50Å" /> | ||
'''Crystal Structure Analysis of an NDP kinase from Pyrobaculum aerophilum'''<br /> | '''Crystal Structure Analysis of an NDP kinase from Pyrobaculum aerophilum'''<br /> | ||
==Overview== | ==Overview== | ||
Nucleoside diphosphate (NDP) kinases are ubiquitous enzymes that transfer | Nucleoside diphosphate (NDP) kinases are ubiquitous enzymes that transfer gamma-phosphates from nucleoside triphosphates to nucleoside diphosphates via a ping-pong mechanism. The important role of this large family of enzymes in controlling cellular functions and developmental processes along with their crystallizability has made them good candidates for structural studies. We recently determined the structure of an evolved version of an NDP kinase from Pyrobaculum aerophilum, an extreme thermophile. This NDP kinase has similarity to the 42 other NDP kinases deposited in the Protein Data Bank (PDB) but differs significantly in sequence, structure, and biophysical properties. The P. aerophilum NDP kinase sequence contains two unique segments not present in other NDP kinases, comprising residues 66-100 and 156-165. We show that deletion mutants of the P. aerophilum NDP kinase lacking either or both of these inserts have an altered substrate specificity, allowing dGTP as the phosphate donor. A structural analysis of the evolved NDP kinase in conjunction with mutagenesis experiments suggests that the substrate specificity of the P. aerophilum NDP kinase is related to the presence of these two inserts. | ||
==About this Structure== | ==About this Structure== | ||
1XQI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrobaculum_aerophilum Pyrobaculum aerophilum] with TRS and PGE as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nucleoside-diphosphate_kinase Nucleoside-diphosphate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.6 2.7.4.6] Full crystallographic information is available from [http:// | 1XQI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrobaculum_aerophilum Pyrobaculum aerophilum] with <scene name='pdbligand=TRS:'>TRS</scene> and <scene name='pdbligand=PGE:'>PGE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nucleoside-diphosphate_kinase Nucleoside-diphosphate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.6 2.7.4.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XQI OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Berendzen, J.]] | [[Category: Berendzen, J.]] | ||
[[Category: Cabantous, S.]] | [[Category: Cabantous, S.]] | ||
[[Category: Liong, E | [[Category: Liong, E C.]] | ||
[[Category: Pedelacq, J | [[Category: Pedelacq, J D.]] | ||
[[Category: Terwilliger, T | [[Category: Terwilliger, T C.]] | ||
[[Category: Waldo, G | [[Category: Waldo, G S.]] | ||
[[Category: PGE]] | [[Category: PGE]] | ||
[[Category: TRS]] | [[Category: TRS]] | ||
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[[Category: ferredoxin fold]] | [[Category: ferredoxin fold]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:57:36 2008'' | ||
Revision as of 16:57, 21 February 2008
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Crystal Structure Analysis of an NDP kinase from Pyrobaculum aerophilum
OverviewOverview
Nucleoside diphosphate (NDP) kinases are ubiquitous enzymes that transfer gamma-phosphates from nucleoside triphosphates to nucleoside diphosphates via a ping-pong mechanism. The important role of this large family of enzymes in controlling cellular functions and developmental processes along with their crystallizability has made them good candidates for structural studies. We recently determined the structure of an evolved version of an NDP kinase from Pyrobaculum aerophilum, an extreme thermophile. This NDP kinase has similarity to the 42 other NDP kinases deposited in the Protein Data Bank (PDB) but differs significantly in sequence, structure, and biophysical properties. The P. aerophilum NDP kinase sequence contains two unique segments not present in other NDP kinases, comprising residues 66-100 and 156-165. We show that deletion mutants of the P. aerophilum NDP kinase lacking either or both of these inserts have an altered substrate specificity, allowing dGTP as the phosphate donor. A structural analysis of the evolved NDP kinase in conjunction with mutagenesis experiments suggests that the substrate specificity of the P. aerophilum NDP kinase is related to the presence of these two inserts.
About this StructureAbout this Structure
1XQI is a Single protein structure of sequence from Pyrobaculum aerophilum with and as ligands. Active as Nucleoside-diphosphate kinase, with EC number 2.7.4.6 Full crystallographic information is available from OCA.
ReferenceReference
Structural and functional features of an NDP kinase from the hyperthermophile crenarchaeon Pyrobaculum aerophilum., Pedelacq JD, Waldo GS, Cabantous S, Liong EC, Terwilliger TC, Protein Sci. 2005 Oct;14(10):2562-73. PMID:16195547
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