1t6d: Difference between revisions

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New page: left|200px<br /><applet load="1t6d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t6d, resolution 2.15Å" /> '''MIRAS phasing of the...
 
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[[Image:1t6d.jpg|left|200px]]<br /><applet load="1t6d" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1t6d.jpg|left|200px]]<br /><applet load="1t6d" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1t6d, resolution 2.15&Aring;" />
caption="1t6d, resolution 2.15&Aring;" />
'''MIRAS phasing of the Aquifex aeolicus Ppx/GppA phosphatase: crystal structure of the type II variant'''<br />
'''MIRAS phasing of the Aquifex aeolicus Ppx/GppA phosphatase: crystal structure of the type II variant'''<br />


==Overview==
==Overview==
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.
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.


==About this Structure==
==About this Structure==
1T6D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus_vf5 Aquifex aeolicus vf5] with CL and TRS as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1T6D OCA].  
1T6D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus_vf5 Aquifex aeolicus vf5] with <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=TRS:'>TRS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T6D OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Gajhede, M.]]
[[Category: Gajhede, M.]]
[[Category: Kastrup, J.S.]]
[[Category: Kastrup, J S.]]
[[Category: Kristensen, O.]]
[[Category: Kristensen, O.]]
[[Category: Laurberg, M.]]
[[Category: Laurberg, M.]]
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[[Category: alpha/beta protein]]
[[Category: alpha/beta protein]]


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