2ltj

</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=2ltj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ltj OCA], [https://pdbe.org/2ltj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ltj RCSB], [https://www.ebi.ac.uk/pdbsum/2ltj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ltj ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Streptococcus pneumoniae is a serious human pathogen that presents on its surface numerous proteins involved in the host-bacterium interaction. The carbohydrate-active enzymes are particularly well represented among these surface proteins, and many of these are known virulence factors, highlighting the importance of carbohydrate processing by this pathogen. StrH is a surface-attached exo-beta-d-N-acetylglucosaminidase that cooperates with the sialidase NanA and the beta-galactosidase BgaA to sequentially degrade the nonreducing terminal arms of complex N-linked glycans. This enzyme is a large multi-modular protein that is notable for its tandem N-terminal family GH20 catalytic modules, whose individual X-ray crystal structures were recently reported. StrH also contains C-terminal tandem G5 modules, which are uncharacterized. Here, we report the NMR-determined solution structure of the first G5 module in the tandem, G5-1, which along with the X-ray crystal structures of the GH20 modules was used in conjunction with small-angle X-ray scattering to construct a pseudo-atomic model of full-length StrH. The results reveal a model in which StrH adopts an elongated conformation that may project the catalytic modules away from the surface of the bacterium to a distance of up to ~250A.

Conformational Analysis of StrH, the Surface-Attached exo-beta-d-N-Acetylglucosaminidase from Streptococcus pneumoniae.,Pluvinage B, Chitayat S, Ficko-Blean E, Abbott DW, Kunjachen JM, Grondin J, Spencer HL, Smith SP, Boraston AB J Mol Biol. 2012 Nov 12. pii: S0022-2836(12)00877-7. doi:, 10.1016/j.jmb.2012.11.005. PMID:23154168<ref>PMID:23154168</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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