5b88: Difference between revisions

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-'''Unreleased structure'''
-The entry 5b88 is ON HOLD  until Paper Publication
+==RRM-like domain of DEAD-box protein, CsdA==
+<StructureSection load='5b88' size='340' side='right'caption='[[5b88]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5b88]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B88 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B88 FirstGlance]. <br>
+</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=5b88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b88 OCA], [https://pdbe.org/5b88 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b88 RCSB], [https://www.ebi.ac.uk/pdbsum/5b88 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b88 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/DEAD_ECOLI DEAD_ECOLI] DEAD-box RNA helicase involved in various cellular processes at low temperature, including ribosome biogenesis, mRNA degradation and translation initiation. Exhibits RNA-stimulated ATP hydrolysis and RNA unwinding activity at low temperature. Involved in 50S ribosomal subunit assembly, acting after SrmB, and could also play a role in the biogenesis of the 30S ribosomal subunit. In addition, is involved in mRNA decay, via formation of a cold-shock degradosome with RNase E. Also stimulates translation of some mRNAs, probably at the level of initiation.[HAMAP-Rule:MF_00964]<ref>PMID:10216955</ref> <ref>PMID:15148362</ref> <ref>PMID:15196029</ref> <ref>PMID:15554978</ref> <ref>PMID:17259309</ref> <ref>PMID:8552679</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+CsdA has been proposed to be essential for the biogenesis of ribosome and gene regulation after cold shock. However, the structure of CsdA and the function of its long C-terminal regions are still unclear. Here, we solved all of the domain structures of CsdA and found two previously uncharacterized auxiliary domains: a dimerization domain (DD) and an RNA-binding domain (RBD). Small-angle X-ray scattering experiments helped to track the conformational flexibilities of the helicase core domains and C-terminal regions. Biochemical assays revealed that DD is indispensable for stabilizing the CsdA dimeric structure. We also demonstrate for the first time that CsdA functions as a stable dimer at low temperature. The C-terminal regions are critical for RNA binding and efficient enzymatic activities. CsdA_RBD could specifically bind to the regions with a preference for single-stranded G-rich RNA, which may help to bring the helicase core to unwind the adjacent duplex.
-Authors:
+Insights into the Structure of Dimeric RNA Helicase CsdA and Indispensable Role of Its C-Terminal Regions.,Xu L, Wang L, Peng J, Li F, Wu L, Zhang B, Lv M, Zhang J, Gong Q, Zhang R, Zuo X, Zhang Z, Wu J, Tang Y, Shi Y Structure. 2017 Dec 5;25(12):1795-1808.e5. doi: 10.1016/j.str.2017.09.013. Epub, 2017 Oct 26. PMID:29107486<ref>PMID:29107486</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5b88" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Helicase 3D structures|Helicase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Escherichia coli K-12]]
+[[Category: Large Structures]]
+[[Category: Peng J]]
+[[Category: Shi Y]]
+[[Category: Tang Y]]
+[[Category: Wu J]]
+[[Category: Xu L]]
+[[Category: Zhang J]]