1enr: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(One intermediate revision by the same user not shown)
Line 3: Line 3:
<StructureSection load='1enr' size='340' side='right'caption='[[1enr]], [[Resolution|resolution]] 1.83&Aring;' scene=''>
<StructureSection load='1enr' size='340' side='right'caption='[[1enr]], [[Resolution|resolution]] 1.83&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1enr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ENR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ENR FirstGlance]. <br>
<table><tr><td colspan='2'>[[1enr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ENR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ENR FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.83&#8491;</td></tr>
<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=1enr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1enr OCA], [http://pdbe.org/1enr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1enr RCSB], [http://www.ebi.ac.uk/pdbsum/1enr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1enr ProSAT]</span></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=ZN:ZINC+ION'>ZN</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=1enr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1enr OCA], [https://pdbe.org/1enr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1enr RCSB], [https://www.ebi.ac.uk/pdbsum/1enr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1enr ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CONA_CANEN CONA_CANEN]] D-mannose specific lectin.  
[https://www.uniprot.org/uniprot/CONA_CANEN CONA_CANEN] D-mannose specific lectin.
== 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=1enr 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=1enr ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The lectin concanavalin A (ConA) sequentially binds a transition metal ion in the metal-binding site S1 and a calcium ion in the metal-binding site S2 to form its saccharide-binding site. Metal-free ConA crystals soaked with either Zn2+ (apoZn-ConA) or Co2+ (apoCo-ConA) display partial binding of these ions in the proto-transition metal-binding site, but no further conformational changes are observed. These structures can represent the very first step in going from metal-free ConA toward the holoprotein. In the co-crystals of metal-free ConA with Zn2+ (Zn-ConA), the zinc ion can fully occupy the S1 site. The positions of the carboxylate ligands Asp10 and Asp19 that bridge the S1 and S2 sites are affected. The ligation to Zn2+ orients Asp10 optimally for calcium ligation and stabilizes Asp19 by a hydrogen bond to one of its water ligands. The neutralizing and stabilizing effect of the binding of Zn2+ in S1 is necessary to allow for subsequent Ca2+ binding in the S2 site. However, the S2 site of monometallized ConA is still disrupted. The co-crystals of metal-free ConA with both Zn2+ and Ca2+ contain the active holoprotein (ConA ZnCa). Ca2+ has induced large conformational changes to stabilize its hepta-coordination in the S2 site, which comprise the trans to cis isomerization of the Ala207-Asp208 peptide bond accompanied by the formation of the saccharide-binding site. The Zn2+ ligation in ConA ZnCa is similar to Mn2+, Cd2+, Co2+, or Ni2+ ligation in the S1 site, in disagreement with earlier extended x-ray absorption fine structure results that suggested a lower coordination number for Zn2+.
Sequential structural changes upon zinc and calcium binding to metal-free concanavalin A.,Bouckaert J, Poortmans F, Wyns L, Loris R J Biol Chem. 1996 Jul 5;271(27):16144-50. PMID:8663112<ref>PMID:8663112</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1enr" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Concanavalin 3D structures|Concanavalin 3D structures]]
*[[Concanavalin 3D structures|Concanavalin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Canavalia ensiformis]]
[[Category: Canavalia ensiformis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bouckaert, J]]
[[Category: Bouckaert J]]
[[Category: Loris, R]]
[[Category: Loris R]]
[[Category: Poortmans, F]]
[[Category: Poortmans F]]
[[Category: Wyns, L]]
[[Category: Wyns L]]
[[Category: Agglutinin]]
[[Category: Concanavalin some]]
[[Category: Plant lectin]]

Latest revision as of 10:05, 7 February 2024

CO-CRYSTALS OF DEMETALLIZED CONCANAVALIN A WITH ZINC AND CALCIUM HAVING A ZINC ION BOUND IN THE S1 SITE AND A CALCIUM ION BOUND IN THE S2 SITECO-CRYSTALS OF DEMETALLIZED CONCANAVALIN A WITH ZINC AND CALCIUM HAVING A ZINC ION BOUND IN THE S1 SITE AND A CALCIUM ION BOUND IN THE S2 SITE

Structural highlights

1enr is a 1 chain structure with sequence from Canavalia ensiformis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.83Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CONA_CANEN D-mannose specific lectin.

Evolutionary Conservation

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

See Also

1enr, resolution 1.83Å

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=1enr&oldid=4042765"