1mvq: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
Line 4: Line 4:
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1mvq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cratylia_mollis Cratylia mollis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MVQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MVQ FirstGlance]. <br>
<table><tr><td colspan='2'>[[1mvq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cratylia_mollis Cratylia mollis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MVQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MVQ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MMA:O1-METHYL-MANNOSE'>MMA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.77&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MMA:O1-METHYL-MANNOSE'>MMA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></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=1mvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mvq OCA], [https://pdbe.org/1mvq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mvq RCSB], [https://www.ebi.ac.uk/pdbsum/1mvq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mvq 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=1mvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mvq OCA], [https://pdbe.org/1mvq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mvq RCSB], [https://www.ebi.ac.uk/pdbsum/1mvq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mvq ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/LEC1_CRAMO LEC1_CRAMO]] Glucose/D-mannose specific lectin.<ref>PMID:8579345</ref>
[https://www.uniprot.org/uniprot/LEC1_CRAMO LEC1_CRAMO] Glucose/D-mannose specific lectin.<ref>PMID:8579345</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 19: Line 20:
</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=1mvq 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=1mvq ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Carbohydrate-protein interactions play a key role in many biological processes. Cramoll is a lectin purified from Cratylia mollis seeds that is taxonomically related to concanavalin A (Con A). Although Cramoll and Con A have the same monosaccharide specificity, they have different glycoprotein binding profiles. We report the primary structure of Cramoll, determined by Edman degradation and mass spectrometry and its 1.77 A crystallographic structure and compare it with the three-dimensional structure of Con A in an attempt to understand how differential binding can be achieved by similar or nearly identical structures. We report here that Cramoll consists of 236 residues, with 82% identity with Con A, and that its topological architecture is essentially identical to Con A, because the Calpha positional differences are below 3.5 A. Cramoll and Con A have identical binding sites for MealphaMan, Mn2+, and Ca2+. However, we observed six substitutions in a groove adjacent to the extended binding site and two in the extended binding site that may explain the differences in binding of oligosaccharides and glycoproteins between Cramoll and Con A.
Amino acid sequence and tertiary structure of Cratylia mollis seed lectin.,De Souza GA, Oliveira PS, Trapani S, Santos AC, Rosa JC, Laure HJ, Faca VM, Correia MT, Tavares GA, Oliva G, Coelho LC, Greene LJ Glycobiology. 2003 Dec;13(12):961-72. Epub 2003 Sep 9. PMID:12966038<ref>PMID:12966038</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1mvq" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
Line 34: Line 26:
[[Category: Cratylia mollis]]
[[Category: Cratylia mollis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Coelho, L C]]
[[Category: Coelho LC]]
[[Category: Correia, M T]]
[[Category: Correia MT]]
[[Category: Greene, L J]]
[[Category: Greene LJ]]
[[Category: Oliva, G]]
[[Category: Oliva G]]
[[Category: Oliveira, P S]]
[[Category: Oliveira PS]]
[[Category: Souza, G A.de]]
[[Category: Trapani S]]
[[Category: Trapani, S]]
[[Category: De Souza GA]]
[[Category: Legume lectin]]
[[Category: Sugar binding protein]]

Latest revision as of 10:49, 14 February 2024

Cratylia mollis lectin (isoform 1) in complex with methyl-alpha-D-mannoseCratylia mollis lectin (isoform 1) in complex with methyl-alpha-D-mannose

Structural highlights

1mvq is a 1 chain structure with sequence from Cratylia mollis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.77Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LEC1_CRAMO Glucose/D-mannose specific lectin.[1]

Evolutionary Conservation

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

References

  1. ↑ Correia MT, Coelho LC. Purification of a glucose/mannose specific lectin, isoform 1, from seeds of Cratylia mollis Mart. (Camaratu bean). Appl Biochem Biotechnol. 1995 Dec;55(3):261-73. PMID:8579345

1mvq, resolution 1.77Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1mvq&oldid=4051909"