This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1uqx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1uqx.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1uqx.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1uqx| PDB=1uqx | SCENE= }}
{{STRUCTURE_1uqx| PDB=1uqx | SCENE= }}
-
'''RALSTONIA SOLANACEARUM LECTIN (RS-IIL) IN COMPLEX WITH ALPHA-METHYLMANNOSIDE'''
+
===RALSTONIA SOLANACEARUM LECTIN (RS-IIL) IN COMPLEX WITH ALPHA-METHYLMANNOSIDE===
-
==Overview==
+
<!--
-
The plant pathogen Ralstonia solanacearum produces two lectins, each with different affinity to fucose. We described previously the properties and sequence of the first lectin, RSL (subunit M(r) 9.9 kDa), which is related to fungal lectins (Sudakevitz, D., Imberty, A., and Gilboa-Garber, N., 2002, J Biochem 132: 353-358). The present communication reports the discovery of the second one, RS-IIL (subunit M(r) 11.6 kDa), a tetrameric lectin, with high sequence similarity to the fucose-binding lectin PA-IIL of Pseudomonas aeruginosa. RS-IIL recognizes fucose but displays much higher affinity to mannose and fructose, which is opposite to the preference spectrum of PA-IIL. Determination of the crystal structure of RS-IIL complexed with a mannose derivative demonstrates a tetrameric structure very similar to the recently solved PA-IIL structure (Mitchell, E., et al., 2002, Nature Struct Biol 9: 918-921). Each monomer contains two close calcium cations that mediate the binding of the monosaccharide and explain the outstandingly high affinity to the monosaccharide ligand. The binding loop of the cations is fully conserved in RS-IIL and PA-IIL, whereas the preference for mannose versus fucose can be attributed to the change of a three-amino-acid sequence in the 'specificity loop'.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15101976}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15101976 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15101976}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Lectin]]
[[Category: Lectin]]
[[Category: Sugar-binding protein]]
[[Category: Sugar-binding protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:34:03 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:35:54 2008''

Revision as of 12:35, 29 July 2008

Image:1uqx.png

Template:STRUCTURE 1uqx

RALSTONIA SOLANACEARUM LECTIN (RS-IIL) IN COMPLEX WITH ALPHA-METHYLMANNOSIDE

Template:ABSTRACT PUBMED 15101976

About this Structure

1UQX is a Single protein structure of sequence from Ralstonia solanacearum. Full crystallographic information is available from OCA.

Reference

A new Ralstonia solanacearum high-affinity mannose-binding lectin RS-IIL structurally resembling the Pseudomonas aeruginosa fucose-specific lectin PA-IIL., Sudakevitz D, Kostlanova N, Blatman-Jan G, Mitchell EP, Lerrer B, Wimmerova M, Katcoff DJ, Imberty A, Gilboa-Garber N, Mol Microbiol. 2004 May;52(3):691-700. PMID:15101976

Page seeded by OCA on Tue Jul 29 15:35:54 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1uqx"
Personal tools