3h72
From Proteopedia
(Difference between revisions)
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<StructureSection load='3h72' size='340' side='right'caption='[[3h72]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='3h72' size='340' side='right'caption='[[3h72]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3h72]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3h72]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_R6 Streptococcus pneumoniae R6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H72 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H72 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">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr> | |
| - | <tr id=' | + | |
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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=3h72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h72 OCA], [https://pdbe.org/3h72 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h72 RCSB], [https://www.ebi.ac.uk/pdbsum/3h72 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h72 ProSAT]</span></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=3h72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h72 OCA], [https://pdbe.org/3h72 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h72 RCSB], [https://www.ebi.ac.uk/pdbsum/3h72 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h72 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/NANA_STRR6 NANA_STRR6] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3h72 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3h72 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Currently there is pressing need to develop novel therapeutic agents for the treatment of infections by the human respiratory pathogens Pseudomonas aeruginosa and Streptococcus pneumoniae. The neuraminidases of these pathogens are important for host colonization in animal models of infection and are attractive targets for drug discovery. To aid in the development of inhibitors against these neuraminidases, we have determined the crystal structures of the P. aeruginosa enzyme NanPs and S. pneumoniae enzyme NanA at 1.6 and 1.7A resolution, respectively. In situ proteolysis with trypsin was essential for the crystallization of our recombinant NanA. The active site regions of the two enzymes are strikingly different. NanA contains a deep pocket that is similar to that in canonical neuraminidases, while the NanPs active site is much more open. The comparative studies suggest that NanPs may not be a classical neuraminidase, and may have distinct natural substrates and physiological functions. This work represents an important step in the development of drugs to prevent respiratory tract colonization by these two pathogens. | ||
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| - | Crystal structures of respiratory pathogen neuraminidases.,Hsiao YS, Parker D, Ratner AJ, Prince A, Tong L Biochem Biophys Res Commun. 2009 Mar 13;380(3):467-71. Epub 2009 Jan 23. PMID:19284989<ref>PMID:19284989</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3h72" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Neuraminidase 3D structures|Neuraminidase 3D structures]] | *[[Neuraminidase 3D structures|Neuraminidase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Exo-alpha-sialidase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Streptococcus pneumoniae R6]] |
| - | [[Category: Hsiao | + | [[Category: Hsiao Y-S]] |
| - | [[Category: Tong | + | [[Category: Tong L]] |
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Current revision
Crystal structure of Streptococcus pneumoniae D39 neuraminidase A precursor (NanA) in complex with NANA
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