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[[Image:2cmg.gif|left|200px]]<br /><applet load="2cmg" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2cmg, resolution 2.00&Aring;" />
'''CRYSTAL STRUCTURE OF SPERMIDINE SYNTHASE FROM HELICOBACTER PYLORI'''<br />


==About this Structure==
==Crystal Structure of Spermidine Synthase from Helicobacter Pylori==
2CMG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Active as [http://en.wikipedia.org/wiki/Spermidine_synthase Spermidine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.16 2.5.1.16] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CMG OCA].
<StructureSection load='2cmg' size='340' side='right'caption='[[2cmg]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
[[Category: Helicobacter pylori]]
== Structural highlights ==
[[Category: Single protein]]
<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>
[[Category: Spermidine synthase]]
</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>
[[Category: Lu, P.K.]]
<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>
[[Category: Sun, Y.J.]]
</table>
[[Category: polyamine biosynthesis]]
== Function ==
[[Category: putrescine aminopropyltransferase]]
[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>
[[Category: spee]]
== Evolutionary Conservation ==
[[Category: spermidine biosynthesis]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: spermidine synthase]]
Check<jmol>
[[Category: transferase]]
  <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.


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:20:05 2008''
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>
 
==See Also==
*[[Spermidine synthase 3D structures|Spermidine synthase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Helicobacter pylori 26695]]
[[Category: Large Structures]]
[[Category: Lu p-k]]
[[Category: Sun y-j]]

Latest revision as of 09:27, 9 May 2024

Crystal Structure of Spermidine Synthase from Helicobacter Pylori

2cmg, resolution 2.00Å

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