1ww4: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ww4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Agrocybe_cylindracea Agrocybe cylindracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WW4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WW4 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ww4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Agrocybe_cylindracea Agrocybe cylindracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WW4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WW4 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</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]] 2.3&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ww5|1ww5]], [[1ww6|1ww6]], [[1ww7|1ww7]]</div></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=1ww4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ww4 OCA], [https://pdbe.org/1ww4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ww4 RCSB], [https://www.ebi.ac.uk/pdbsum/1ww4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ww4 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=1ww4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ww4 OCA], [https://pdbe.org/1ww4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ww4 RCSB], [https://www.ebi.ac.uk/pdbsum/1ww4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ww4 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ATLE_CYCAE ATLE_CYCAE] Anti-tumor lectin with DNase activity. Inhibits the growth of several tumor cell lines in vitro. Induces lymphocyte infiltration and necrosis of tumor cells in a mouse tumor model. Induces apoptosis in HeLa cells. Binds N-acetylneuraminyl lactose (N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->4)-beta-D-glucose) (PubMed:16051274).<ref>PMID:12757412</ref> <ref>PMID:16051274</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1ww4 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=1ww4 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Galectin from an edible fungus Agrocybe cylindracea (ACG) has a strong preference for N-acetylneuraminyl lactose (NeuAcalpha2-3lactose). The sugar recognition mechanism of ACG was explored by the X-ray crystallographic analyses of ligand-free ACG, and its complex with lactose, 3'-sulfonyl lactose and NeuAcalpha2-3lactose. The refined structure shows that ACG is a "proto"-type galectin composed of a beta-sandwich of two antiparallel sheets, each with six strands, in contrast to the five and six strands in animal galectins. ACG dimer in solution was classified as being among the "layer"-type. The carbohydrate recognition domain (CRD) of this galectin is common to those of animal galectins, except for substitution of one residue, Ala64, which corresponds to Asn46 in human galectin 1. A five-residue insertion in ACG at positions 42-46 involving Ser44 and Asn46 modified the architecture of the sugar binding site that contributes sialic acid specificity. Furthermore, it was found that the binding of a sulfate ion near the CRD in the ligand-free form led to a change in the conformation of the loop region caused by main-chain cis/trans transition between Ser44 and Pro45.
Structural basis of a fungal galectin from Agrocybe cylindracea for recognizing sialoconjugate.,Ban M, Yoon HJ, Demirkan E, Utsumi S, Mikami B, Yagi F J Mol Biol. 2005 Aug 26;351(4):695-706. PMID:16051274<ref>PMID:16051274</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ww4" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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[[Category: Agrocybe cylindracea]]
[[Category: Agrocybe cylindracea]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ban, M]]
[[Category: Ban M]]
[[Category: Demirkan, E]]
[[Category: Demirkan E]]
[[Category: Mikami, B]]
[[Category: Mikami B]]
[[Category: Utsumi, S]]
[[Category: Utsumi S]]
[[Category: Yagi, F]]
[[Category: Yagi F]]
[[Category: Yoon, H J]]
[[Category: Yoon HJ]]
[[Category: Agrocybe cylindracea galectin]]
[[Category: Carbohydrate recognition domain]]
[[Category: Fungal galectin]]
[[Category: N-acetylneuraminyl lactose]]
[[Category: Sugar binding protein]]
[[Category: X-ray crystallographic analysis]]

Latest revision as of 16:34, 13 March 2024

Agrocybe cylindracea galectin complexed with NeuAca2-3lactoseAgrocybe cylindracea galectin complexed with NeuAca2-3lactose

Structural highlights

1ww4 is a 4 chain structure with sequence from Agrocybe cylindracea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ATLE_CYCAE Anti-tumor lectin with DNase activity. Inhibits the growth of several tumor cell lines in vitro. Induces lymphocyte infiltration and necrosis of tumor cells in a mouse tumor model. Induces apoptosis in HeLa cells. Binds N-acetylneuraminyl lactose (N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->4)-beta-D-glucose) (PubMed:16051274).[1] [2]

Evolutionary Conservation

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

See Also

References

  1. ↑ Zhao C, Sun H, Tong X, Qi Y. An antitumour lectin from the edible mushroom Agrocybe aegerita. Biochem J. 2003 Sep 1;374(Pt 2):321-7. PMID:12757412 doi:10.1042/BJ20030300
  2. ↑ Ban M, Yoon HJ, Demirkan E, Utsumi S, Mikami B, Yagi F. Structural basis of a fungal galectin from Agrocybe cylindracea for recognizing sialoconjugate. J Mol Biol. 2005 Aug 26;351(4):695-706. PMID:16051274 doi:10.1016/j.jmb.2005.06.045

1ww4, resolution 2.30Å

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