1hcx

From Proteopedia

(Difference between revisions)

Revision as of 14:22, 24 December 2014

CHOLINE BINDING DOMAIN OF THE MAJOR AUTOLYSIN (C-LYTA) FROM STREPTOCOCCUS PNEUMONIAE

Structural highlights

1hcx is a 2 chain structure with sequence from Streptococcus pneumoniae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1h8g
Gene:	LYTA (Streptococcus pneumoniae)
Activity:	N-acetylmuramoyl-L-alanine amidase, with EC number 3.5.1.28
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Fernandez-Tornero C, Lopez R, Garcia E, Gimenez-Gallego G, Romero A. A novel solenoid fold in the cell wall anchoring domain of the pneumococcal virulence factor LytA. Nat Struct Biol. 2001 Dec;8(12):1020-4. PMID:11694890 doi:10.1038/nsb724

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1hcx"

@@ Line 9: / Line 9: @@
 <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=1hcx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hcx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hcx RCSB], [http://www.ebi.ac.uk/pdbsum/1hcx PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1hcx

From Proteopedia

Revision as of 14:22, 24 December 2014

CHOLINE BINDING DOMAIN OF THE MAJOR AUTOLYSIN (C-LYTA) FROM STREPTOCOCCUS PNEUMONIAE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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