1mky

From Proteopedia

(Difference between revisions)

Revision as of 10:04, 7 February 2015

Structural Analysis of the Domain Interactions in Der, a Switch Protein Containing Two GTPase Domains

Structural highlights

1mky is a 1 chain structure with sequence from Atcc 43589. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[DER_THEMA] GTPase that plays an essential role in the late steps of ribosome biogenesis (By similarity). Has GTPase activity but no ATPase activity. GTP, GDP, and dGTP but not GMP, ATP, CTP, and UTP compete for GTP binding.[HAMAP-Rule:MF_00195]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The EngA subfamily of essential bacterial GTPases has a unique domain structure consisting of two adjacent GTPase domains (GD1 and GD2) and a C-terminal domain. The structure of Thermotoga maritima Der bound to GDP determined at 1.9 A resolution reveals a novel domain arrangement in which the GTPase domains pack at either side of the C-terminal domain. Unexpectedly, the C-terminal domain resembles a KH domain, missing the distinctive RNA recognition elements. Conserved motifs of the nucleotide binding site of GD1 are integral parts of the GD1-KH domain interface, suggesting the interactions between these two domains are directly influenced by the GTP/GDP cycling of the protein. In contrast, the GD2-KH domain interface is distal to the GDP binding site of GD2.

Domain arrangement of Der, a switch protein containing two GTPase domains.,Robinson VL, Hwang J, Fox E, Inouye M, Stock AM Structure. 2002 Dec;10(12):1649-58. PMID:12467572^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Robinson VL, Hwang J, Fox E, Inouye M, Stock AM. Domain arrangement of Der, a switch protein containing two GTPase domains. Structure. 2002 Dec;10(12):1649-58. PMID:12467572

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1mky"

@@ Line 2: / Line 2: @@
 <StructureSection load='1mky' size='340' side='right' caption='[[1mky]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1mky]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MKY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MKY FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1mky]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MKY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MKY FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
@@ Line 31: / Line 31: @@
 __TOC__
 </StructureSection>
-[[Category: Thermotoga maritima]]
+[[Category: Atcc 43589]]
 [[Category: Fox, E]]
 [[Category: Hwang, J]]

1mky

From Proteopedia

Revision as of 10:04, 7 February 2015

Structural Analysis of the Domain Interactions in Der, a Switch Protein Containing Two GTPase Domains

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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