View source for 3enu


==Crystal structure of Nitrollin, a betagamma-crystallin from Nitrosospira multiformis==
<StructureSection load='3enu' size='340' side='right'caption='[[3enu]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3enu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Nitrosospira_multiformis_ATCC_25196 Nitrosospira multiformis ATCC 25196]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ENU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ENU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.86&#8491;</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=3enu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3enu OCA], [https://pdbe.org/3enu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3enu RCSB], [https://www.ebi.ac.uk/pdbsum/3enu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3enu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q2YAE2_NITMU Q2YAE2_NITMU] 
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== Publication Abstract from PubMed ==
The betagamma-crystallin superfamily has a well-characterized protein fold, with several members found in both prokaryotic and eukaryotic worlds. A majority of them contain two betagamma-crystallin domains. A few examples, such as ciona crystallin and spherulin 3a exist that represent the eukaryotic single-domain proteins of this superfamily. This study reports the high-resolution crystal structure of a single-domain betagamma-crystallin protein, nitrollin, from the ammonium-oxidizing soil bacterium Nitrosospira multiformis. The structure retains the characteristic betagamma-crystallin fold despite a very low sequence identity. The protein exhibits a unique case of homodimerization in betagamma-crystallins by employing its N-terminal extension to undergo three-dimensional (3D) domain swapping with its partner. Removal of the swapped strand results in partial loss of structure and stability but not dimerization per se as determined using gel filtration and equilibrium unfolding studies. Overall, nitrollin represents a distinct single-domain prokaryotic member that has evolved a specialized mode of dimerization hitherto unknown in the realm of betagamma-crystallins.

Three-dimensional domain swapping in nitrollin, a single-domain betagamma-crystallin from Nitrosospira multiformis, controls protein conformation and stability but not dimerization.,Aravind P, Suman SK, Mishra A, Sharma Y, Sankaranarayanan R J Mol Biol. 2009 Jan 9;385(1):163-77. Epub 2008 Oct 19. PMID:18976659<ref>PMID:18976659</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Nitrosospira multiformis ATCC 25196]]
[[Category: Aravind P]]
[[Category: Sankaranarayanan R]]