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==SOLUTION STRUCTURE OF TACHYCITIN, AN ANTIMICROBIAL PROTEIN WITH CHITIN-BINDING FUNCTION==
==SOLUTION STRUCTURE OF TACHYCITIN, AN ANTIMICROBIAL PROTEIN WITH CHITIN-BINDING FUNCTION==
<StructureSection load='1dqc' size='340' side='right'caption='[[1dqc]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''>
<StructureSection load='1dqc' size='340' side='right'caption='[[1dqc]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1dqc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tachypleus_tridentatus Tachypleus tridentatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DQC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DQC FirstGlance]. <br>
<table><tr><td colspan='2'>[[1dqc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tachypleus_tridentatus Tachypleus tridentatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DQC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DQC FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</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=1dqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dqc OCA], [https://pdbe.org/1dqc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dqc RCSB], [https://www.ebi.ac.uk/pdbsum/1dqc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dqc 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=1dqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dqc OCA], [https://pdbe.org/1dqc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dqc RCSB], [https://www.ebi.ac.uk/pdbsum/1dqc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dqc ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/P91818_TACTR P91818_TACTR]
== 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=1dqc 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=1dqc ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Tachycitin, a 73-residue polypeptide having antimicrobial activity is present in the hemocyte of horseshoe crab (Tachypleus tridentatus). The first three-dimensional structure of invertebrate chitin-binding protein was determined for tachycitin using two-dimensional nuclear magnetic resonance spectroscopy. The measurements indicate that the structure of tachycitin is largely divided into N- and C-terminal domains; the former comprises a three-stranded beta-sheet and the latter a two-stranded beta-sheet following a short helical turn. The latter structural motif shares a significant tertiary structural similarity with the chitin-binding domain of plant chitin-binding protein. This result is thought to provide faithful experimental evidence to the recent hypothesis that chitin-binding proteins of invertebrates and plants are correlated by a convergent evolution process.
Chitin-binding proteins in invertebrates and plants comprise a common chitin-binding structural motif.,Suetake T, Tsuda S, Kawabata S, Miura K, Iwanaga S, Hikichi K, Nitta K, Kawano K J Biol Chem. 2000 Jun 16;275(24):17929-32. PMID:10770921<ref>PMID:10770921</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1dqc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Tachypleus tridentatus]]
[[Category: Tachypleus tridentatus]]
[[Category: Kawabata, S]]
[[Category: Kawabata S]]
[[Category: Kawano, K]]
[[Category: Kawano K]]
[[Category: Miura, K]]
[[Category: Miura K]]
[[Category: Suetake, T]]
[[Category: Suetake T]]
[[Category: Tsuda, S]]
[[Category: Tsuda S]]
[[Category: Antimicrobial protein]]
[[Category: Disulfide-rich]]

Revision as of 12:52, 20 March 2024

SOLUTION STRUCTURE OF TACHYCITIN, AN ANTIMICROBIAL PROTEIN WITH CHITIN-BINDING FUNCTIONSOLUTION STRUCTURE OF TACHYCITIN, AN ANTIMICROBIAL PROTEIN WITH CHITIN-BINDING FUNCTION

Structural highlights

1dqc is a 1 chain structure with sequence from Tachypleus tridentatus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

P91818_TACTR

Evolutionary Conservation

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

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OCA
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