2zyc: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
 
(10 intermediate revisions by the same user not shown)
Line 1: Line 1:
{{Seed}}
[[Image:2zyc.jpg|left|200px]]


<!--
==Crystal structure of peptidoglycan hydrolase from Sphingomonas sp. A1==
The line below this paragraph, containing "STRUCTURE_2zyc", creates the "Structure Box" on the page.
<StructureSection load='2zyc' size='340' side='right'caption='[[2zyc]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2zyc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingomonas_sp._A1 Sphingomonas sp. A1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZYC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZYC FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.74&#8491;</td></tr>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
{{STRUCTURE_2zyc|  PDB=2zyc  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2zyc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zyc OCA], [https://pdbe.org/2zyc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zyc RCSB], [https://www.ebi.ac.uk/pdbsum/2zyc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zyc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B7XH69_9SPHN B7XH69_9SPHN]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zy/2zyc_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2zyc ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Glycoside hydrolase (GH) categorized into family 73 plays an important role in degrading bacterial cell wall peptidoglycan. The flagellar protein FlgJ contains N- and C-terminal domains responsible for flagellar rod assembly and peptidoglycan hydrolysis, respectively. A member of family GH-73, the C-terminal domain (SPH1045-C) of FlgJ from Sphingomonas sp. strain A1 was expressed in Escherichia coli, purified, and characterized. SPH1045-C exhibited bacterial cell lytic activity most efficiently at pH 6.0 and 37 degrees C. The X-ray crystallographic structure of SPH1045-C was determined at 1.74 A resolution by single-wavelength anomalous diffraction. The enzyme consists of two lobes, alpha and beta. A deep cleft located between the two lobes can accommodate polymer molecules, suggesting that the active site is located in the cleft. Although SPH1045-C shows a structural homology with family GH-22 and GH-23 lysozymes, the arrangement of the nucleophile/base residue in the active site is specific to each peptidoglycan hydrolase.


===Crystal structure of peptidoglycan hydrolase from Sphingomonas sp. A1===
Crystal structure of the glycosidase family 73 peptidoglycan hydrolase FlgJ.,Hashimoto W, Ochiai A, Momma K, Itoh T, Mikami B, Maruyama Y, Murata K Biochem Biophys Res Commun. 2009 Mar 27;381(1):16-21. Epub 2009 Feb 7. PMID:19351587<ref>PMID:19351587</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
==About this Structure==
</div>
2ZYC is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Sphingomonas_sp._a1 Sphingomonas sp. a1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZYC OCA].
<div class="pdbe-citations 2zyc" style="background-color:#fffaf0;"></div>
[[Category: Sphingomonas sp. a1]]
== References ==
[[Category: Hashimoto, W.]]
<references/>
[[Category: Mikami, B.]]
__TOC__
[[Category: Murata, K.]]
</StructureSection>
[[Category: Ochiai, A.]]
[[Category: Large Structures]]
[[Category: Hydrolase]]
[[Category: Sphingomonas sp. A1]]
 
[[Category: Hashimoto W]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb  4 11:24:35 2009''
[[Category: Mikami B]]
[[Category: Murata K]]
[[Category: Ochiai A]]
Retrieved from "https://proteopedia.org/2zyc"