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4dct

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Current revision (14:31, 14 March 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4dct]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DCT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DCT FirstGlance]. <br>
<table><tr><td colspan='2'>[[4dct]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DCT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DCT FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4dct FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dct OCA], [https://pdbe.org/4dct PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dct RCSB], [https://www.ebi.ac.uk/pdbsum/4dct PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dct ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4dct FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dct OCA], [https://pdbe.org/4dct PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dct RCSB], [https://www.ebi.ac.uk/pdbsum/4dct PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dct ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/DER_BACSU DER_BACSU]] GTPase that plays an essential role in the late steps of ribosome biogenesis.<ref>PMID:16997968</ref>
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[https://www.uniprot.org/uniprot/DER_BACSU DER_BACSU] GTPase that plays an essential role in the late steps of ribosome biogenesis.<ref>PMID:16997968</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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EngA proteins form a unique family of bacterial GTPases with two GTP-binding domains in tandem, namely GD1 and GD2, followed by a KH (K-homology) domain. They have been shown to interact with the bacterial ribosome and to be involved in its biogenesis. Most prokaryotic EngA possess a high GTPase activity in contrast to eukaryotic GTPases that act mainly as molecular switches. Here, we have purified and characterized the GTPase activity of the Bacillus subtilis EngA and two shortened EngA variants that only contain GD1 or GD2-KH. Interestingly, the GTPase activity of GD1 alone is similar to that of the whole EngA, whereas GD2-KH has a 150-fold lower GTPase activity. At physiological concentration, potassium strongly stimulates the GTPase activity of each protein construct. Interestingly, it affects neither the affinities for nucleotides nor the monomeric status of EngA or the GD1 domain. Thus, potassium likely acts as a chemical GTPase-activating element as proposed for another bacterial GTPase like MnmE. However, unlike MnmE, potassium does not promote dimerization of EngA. In addition, we solved two crystal structures of full-length EngA. One of them contained for the first time a GTP-like analogue bound to GD2 while GD1 was free. Surprisingly, its overall fold was similar to a previously solved structure with GDP bound to both sites. Our data indicate that a significant structural change must occur upon K(+) binding to GD2, and a comparison with T. maritima EngA and MnmE structures allowed us to propose a model explaining the chemical basis for the different GTPase activities of GD1 and GD2.
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Potassium Acts as a GTPase-Activating Element on Each Nucleotide-Binding Domain of the Essential Bacillus subtilis EngA.,Foucher AE, Reiser JB, Ebel C, Housset D, Jault JM PLoS One. 2012;7(10):e46795. doi: 10.1371/journal.pone.0046795. Epub 2012 Oct 8. PMID:23056455<ref>PMID:23056455</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4dct" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==

Current revision

Crystal Structure of B. subtilis EngA in complex with half-occupacy GDP

PDB ID 4dct

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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