1j57: Difference between revisions
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==NuiA== | ==NuiA== | ||
<StructureSection load='1j57' size='340' side='right'caption='[[1j57 | <StructureSection load='1j57' size='340' side='right'caption='[[1j57]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1j57]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1j57]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc_sp._PCC_7120_=_FACHB-418 Nostoc sp. PCC 7120 = FACHB-418]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J57 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J57 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1j57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j57 OCA], [https://pdbe.org/1j57 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j57 RCSB], [https://www.ebi.ac.uk/pdbsum/1j57 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j57 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q7A260_NOSS1 Q7A260_NOSS1] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: DeRose | [[Category: Nostoc sp. PCC 7120 = FACHB-418]] | ||
[[Category: Kirby | [[Category: DeRose EF]] | ||
[[Category: Lebetkin | [[Category: Kirby TW]] | ||
[[Category: London | [[Category: Lebetkin MS]] | ||
[[Category: Meiss | [[Category: London RE]] | ||
[[Category: Mueller | [[Category: Meiss G]] | ||
[[Category: Pingoud | [[Category: Mueller GA]] | ||
[[Category: Pingoud A]] | |||
Latest revision as of 02:42, 28 December 2023
NuiANuiA
Structural highlights
FunctionPublication Abstract from PubMedNuclease A (NucA) from Anabaena sp. is a non-specific endonuclease able to degrade single and double-stranded DNA and RNA. The endonucleolytic activity is inhibited by the nuclease A inhibitor (NuiA), which binds to NucA with 1:1 stoichiometry and picomolar affinity. In order to better understand the mechanism of inhibition, the solution structure of NuiA was determined by NMR methods. The fold of NuiA is an alpha-beta-alpha sandwich but standard database searches by DALI and TOP revealed no structural homologies. A visual inspection of alpha-beta-alpha folds in the CATH database revealed similarities to the PR-1-like fold (SCOP nomenclature). The similarities include the ordering of secondary structural elements, a single helix on one face of the alpha-beta-alpha sandwich, and three helices on the other face. However, a major difference is in the IV helix, which in the PR-1 fold is short and perpendicular to the I and III helices, but in NuiA is long and parallel to the I and III helices. Additionally, a strand insertion in the beta-sheet makes the NuiA beta-sheet completely antiparallel in organization. The fast time-scale motions of NuiA, characterized by enhanced flexibility of the extended loop between helices III and IV, also show similarities to P14a, which is a PR-1 fold. We propose that the purpose of the PR-1 fold is to form a stable scaffold to present this extended structure for biological interactions with other proteins. This hypothesis is supported by data that show that when NuiA is bound to NucA significant changes in chemical shift occur in the extended loop between helices III and IV. The nuclease A inhibitor represents a new variation of the rare PR-1 fold.,Kirby TW, Mueller GA, DeRose EF, Lebetkin MS, Meiss G, Pingoud A, London RE J Mol Biol. 2002 Jul 19;320(4):771-82. PMID:12095254[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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