2cmg: Difference between revisions

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{{Seed}}
[[Image:2cmg.png|left|200px]]


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==Crystal Structure of Spermidine Synthase from Helicobacter Pylori==
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<StructureSection load='2cmg' size='340' side='right'caption='[[2cmg]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2cmg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CMG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CMG 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]] 2&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2cmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cmg OCA], [https://pdbe.org/2cmg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cmg RCSB], [https://www.ebi.ac.uk/pdbsum/2cmg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cmg ProSAT]</span></td></tr>
{{STRUCTURE_2cmg|  PDB=2cmg  |  SCENE=  }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/SPEE_HELPY SPEE_HELPY] Catalyzes the production of spermidine from putrescine and decarboxylated S-adenosylmethionine (dcSAM), which serves as an aminopropyl donor.<ref>PMID:16009566</ref>
== 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/cm/2cmg_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=2cmg ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Spermidine synthase (putrescine aminopropyltransferase, PAPT) catalyzes the transfer of the aminopropyl group from decarboxylated S-adenosylmethionine to putrescine during spermidine biosynthesis. Helicobacter pylori PAPT (HpPAPT) has a low sequence identity with other PAPTs and lacks the signature sequence found in other PAPTs. The crystal structure of HpPAPT, determined by multiwavelength anomalous dispersion, revealed an N-terminal beta-stranded domain and a C-terminal Rossmann-like domain. Structural comparison with other PAPTs showed that HpPAPT has a unique binding pocket between two domains, numerous non-conserved residues, a less acidic electrostatic surface potential, and a large buried space within the structure. HpPAPT lacks the gatekeeping loop that facilitates substrate binding in other PAPTs. PAPTs are essential for bacterial cell viability; thus, HpPAPT may be a potential antimicrobial drug target for H. pylori owing to its characteristic PAPT sequence and distinct conformation.


===CRYSTAL STRUCTURE OF SPERMIDINE SYNTHASE FROM HELICOBACTER PYLORI===
Crystal structure of Helicobacter pylori spermidine synthase: a Rossmann-like fold with a distinct active site.,Lu PK, Tsai JY, Chien HY, Huang H, Chu CH, Sun YJ Proteins. 2007 May 15;67(3):743-54. PMID:17357156<ref>PMID:17357156</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2cmg" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_17357156}}, adds the Publication Abstract to the page
*[[Spermidine synthase 3D structures|Spermidine synthase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 17357156 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_17357156}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Helicobacter pylori 26695]]
2CMG is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CMG OCA].
[[Category: Large Structures]]
 
[[Category: Lu p-k]]
==Reference==
[[Category: Sun y-j]]
<ref group="xtra">PMID:17357156</ref><references group="xtra"/>
[[Category: Helicobacter pylori]]
[[Category: Spermidine synthase]]
[[Category: Lu, P K.]]
[[Category: Sun, Y J.]]
[[Category: Polyamine biosynthesis]]
[[Category: Putrescine aminopropyltransferase]]
[[Category: Spee]]
[[Category: Spermidine biosynthesis]]
[[Category: Spermidine synthase]]
[[Category: Transferase]]
 
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Retrieved from "https://proteopedia.org/2cmg"