2ltj

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==Conformational analysis of StrH, the surface-attached exo- beta-D-N-acetylglucosaminidase from Streptococcus pneumoniae==
==Conformational analysis of StrH, the surface-attached exo- beta-D-N-acetylglucosaminidase from Streptococcus pneumoniae==
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<StructureSection load='2ltj' size='340' side='right' caption='[[2ltj]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''>
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<StructureSection load='2ltj' size='340' side='right'caption='[[2ltj]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2ltj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LTJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LTJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2ltj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LTJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LTJ FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">strH, SP_0057 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1313 Streptococcus pneumoniae])</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">Solution NMR</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </span></td></tr>
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<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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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ltj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ltj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ltj RCSB], [http://www.ebi.ac.uk/pdbsum/2ltj PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/STRH_STRPN STRH_STRPN]
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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.
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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>
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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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==See Also==
==See Also==
*[[Beta-Hexosaminidase|Beta-Hexosaminidase]]
*[[Beta-Hexosaminidase|Beta-Hexosaminidase]]
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== References ==
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*[[Beta-Hexosaminidase 3D structures|Beta-Hexosaminidase 3D structures]]
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<references/>
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*[[Beta-N-acetylhexosaminidase 3D structures|Beta-N-acetylhexosaminidase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Beta-N-acetylhexosaminidase]]
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[[Category: Large Structures]]
[[Category: Streptococcus pneumoniae]]
[[Category: Streptococcus pneumoniae]]
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[[Category: Abbott, D]]
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[[Category: Abbott D]]
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[[Category: Boraston, A]]
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[[Category: Boraston A]]
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[[Category: Chitayat, S]]
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[[Category: Chitayat S]]
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[[Category: Ficko-Blean, E]]
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[[Category: Ficko-Blean E]]
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[[Category: Grondin, J]]
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[[Category: Grondin J]]
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[[Category: Kunjachen, J]]
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[[Category: Kunjachen J]]
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[[Category: Pluvinage, B]]
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[[Category: Pluvinage B]]
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[[Category: Smith, S]]
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[[Category: Smith S]]
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[[Category: Spencer, H]]
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[[Category: Spencer H]]
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[[Category: B-sheet]]
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[[Category: Elongated]]
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[[Category: Hydrolase]]
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Current revision

Conformational analysis of StrH, the surface-attached exo- beta-D-N-acetylglucosaminidase from Streptococcus pneumoniae

PDB ID 2ltj

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