1hcx

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{{Seed}}
 
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[[Image:1hcx.png|left|200px]]
 
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==Choline binding domain of the major autolysin (C-LytA) from Streptococcus pneumoniae==
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The line below this paragraph, containing "STRUCTURE_1hcx", creates the "Structure Box" on the page.
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<StructureSection load='1hcx' size='340' side='right'caption='[[1hcx]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1hcx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HCX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HCX FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CHT:CHOLINE+ION'>CHT</scene>, <scene name='pdbligand=DDQ:DECYLAMINE-N,N-DIMETHYL-N-OXIDE'>DDQ</scene>, <scene name='pdbligand=TPT:2,2 6,2-TERPYRIDINE+PLATINUM(II)+CHLORIDE'>TPT</scene></td></tr>
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{{STRUCTURE_1hcx| PDB=1hcx | SCENE= }}
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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=1hcx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hcx OCA], [https://pdbe.org/1hcx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hcx RCSB], [https://www.ebi.ac.uk/pdbsum/1hcx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hcx ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ALYS_STRPN ALYS_STRPN] Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella and sporulation. Autolysin strictly depends on the presence of choline-containing cell walls for activity.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hc/1hcx_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1hcx ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Choline binding proteins are virulence determinants present in several Gram-positive bacteria. Because anchorage of these proteins to the cell wall through their choline binding domain is essential for bacterial virulence, their release from the cell surface is considered a powerful target for a weapon against these pathogens. The first crystal structure of a choline binding domain, from the toxin-releasing enzyme pneumococcal major autolysin (LytA), reveals a novel solenoid fold consisting exclusively of beta-hairpins that stack to form a left-handed superhelix. This unique structure is maintained by choline molecules at the hydrophobic interface of consecutive hairpins and may be present in other choline binding proteins that share high homology to the repeated motif of the domain.
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===CHOLINE BINDING DOMAIN OF THE MAJOR AUTOLYSIN (C-LYTA) FROM STREPTOCOCCUS PNEUMONIAE===
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A novel solenoid fold in the cell wall anchoring domain of the pneumococcal virulence factor LytA.,Fernandez-Tornero C, Lopez R, Garcia E, Gimenez-Gallego G, Romero A Nat Struct Biol. 2001 Dec;8(12):1020-4. PMID:11694890<ref>PMID:11694890</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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The line below this paragraph, {{ABSTRACT_PUBMED_11694890}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1hcx" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 11694890 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11694890}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1HCX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HCX OCA].
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==Reference==
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A novel solenoid fold in the cell wall anchoring domain of the pneumococcal virulence factor LytA., Fernandez-Tornero C, Lopez R, Garcia E, Gimenez-Gallego G, Romero A, Nat Struct Biol. 2001 Dec;8(12):1020-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11694890 11694890]
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[[Category: N-acetylmuramoyl-L-alanine amidase]]
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[[Category: Single protein]]
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[[Category: Streptococcus pneumoniae]]
[[Category: Streptococcus pneumoniae]]
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[[Category: Fernandez-Tornero, C.]]
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[[Category: Fernandez-Tornero C]]
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[[Category: Garcia, E.]]
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[[Category: Garcia E]]
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[[Category: Gimenez-Gallego, G.]]
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[[Category: Gimenez-Gallego G]]
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[[Category: Lopez, R.]]
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[[Category: Lopez R]]
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[[Category: Romero, A.]]
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[[Category: Romero A]]
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[[Category: Cell wall attachment]]
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[[Category: Choline-binding domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:00:21 2008''
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Current revision

Choline binding domain of the major autolysin (C-LytA) from Streptococcus pneumoniae

PDB ID 1hcx

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OCA

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