1xd6

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:1xd6.gif|left|200px]]
[[Image:1xd6.gif|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 1xd6 |SIZE=350|CAPTION= <scene name='initialview01'>1xd6</scene>, resolution 2.00&Aring;
+
The line below this paragraph, containing "STRUCTURE_1xd6", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY=
+
or leave the SCENE parameter empty for the default display.
-
|GENE=
+
-->
-
|DOMAIN=
+
{{STRUCTURE_1xd6| PDB=1xd6 | SCENE= }}
-
|RELATEDENTRY=[[1xd5|1XD5]]
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xd6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xd6 OCA], [http://www.ebi.ac.uk/pdbsum/1xd6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xd6 RCSB]</span>
+
-
}}
+
'''Crystal structures of novel monomeric monocot mannose-binding lectins from Gastrodia elata'''
'''Crystal structures of novel monomeric monocot mannose-binding lectins from Gastrodia elata'''
Line 19: Line 16:
==About this Structure==
==About this Structure==
-
1XD6 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Gastrodia_elata Gastrodia elata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XD6 OCA].
+
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XD6 OCA].
==Reference==
==Reference==
Structural mechanism governing the quaternary organization of monocot mannose-binding lectin revealed by the novel monomeric structure of an orchid lectin., Liu W, Yang N, Ding J, Huang RH, Hu Z, Wang DC, J Biol Chem. 2005 Apr 15;280(15):14865-76. Epub 2005 Jan 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15649901 15649901]
Structural mechanism governing the quaternary organization of monocot mannose-binding lectin revealed by the novel monomeric structure of an orchid lectin., Liu W, Yang N, Ding J, Huang RH, Hu Z, Wang DC, J Biol Chem. 2005 Apr 15;280(15):14865-76. Epub 2005 Jan 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15649901 15649901]
-
[[Category: Gastrodia elata]]
 
-
[[Category: Protein complex]]
 
[[Category: Hu, Z.]]
[[Category: Hu, Z.]]
[[Category: Huang, R H.]]
[[Category: Huang, R H.]]
Line 31: Line 26:
[[Category: Wang, M.]]
[[Category: Wang, M.]]
[[Category: Yang, N.]]
[[Category: Yang, N.]]
-
[[Category: antifungal protein]]
+
[[Category: Antifungal protein]]
-
[[Category: homogeneous beta-sheet]]
+
[[Category: Homogeneous beta-sheet]]
-
[[Category: monocot mannose-binding lectin]]
+
[[Category: Monocot mannose-binding lectin]]
-
[[Category: monomer]]
+
[[Category: Monomer]]
-
 
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:52:46 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:47:59 2008''
+

Revision as of 11:52, 3 May 2008

Template:STRUCTURE 1xd6

Crystal structures of novel monomeric monocot mannose-binding lectins from Gastrodia elata


Overview

Two isoforms of an antifungal protein, gastrodianin, were isolated from two subspecies of the orchid Gastrodia elata, belonging to the protein superfamily of monocot mannose-specific lectins. In the context that all available structures in this superfamily are oligomers so far, the crystal structures of the orchid lectins, both at 2.0 A, revealed a novel monomeric structure. It resulted from the rearrangement of the C-terminal peptide inclusive of the 12th beta-strand, which changes from the "C-terminal exchange" into a "C-terminal self-assembly" mode. Thus, the overall tertiary scaffold is stabilized with an intramolecular beta-sheet instead of the hybrid observed on subunit/subunit interface in all known homologous dimeric or tetrameric lectins. In contrast to the constrained extended conformation with a cis peptide bond between residues 98 and 99 commonly occurring in oligomers, a beta-hairpin forms from position 97 to 101 with a normal trans peptide bond at the corresponding site in gastrodianin, which determines the topology of the C-terminal peptide and thereby its unique fold pattern. Sequence and structure comparison shows that residue replacement and insertion at the position where the beta-hairpin occurs in association with cis-trans inter-conversion of the specific peptide bond (97-98) are possibly responsible for such a radical structure switch between monomers and oligomers. Moreover, this seems to be a common melody controlling the quaternary states among bulb lectins through studies on sequence alignment. The observations revealed a structural mechanism by which the quaternary organization of monocot mannose binding lectins could be governed. The mutation experiment performed on maltose-binding protein-gastrodianin fusion protein followed by a few biochemical detections provides direct evidence to support this conclusion. Potential carbohydrate recognition sites and biological implications of the orchid lectin based on its monomeric state are also discussed in this paper.

About this Structure

Full crystallographic information is available from OCA.

Reference

Structural mechanism governing the quaternary organization of monocot mannose-binding lectin revealed by the novel monomeric structure of an orchid lectin., Liu W, Yang N, Ding J, Huang RH, Hu Z, Wang DC, J Biol Chem. 2005 Apr 15;280(15):14865-76. Epub 2005 Jan 13. PMID:15649901 Page seeded by OCA on Sat May 3 14:52:46 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools