This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2h5a

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="2h5a" size="450" color="white" frame="true" align="right" spinBox="true" caption="2h5a, resolution 1.72&Aring;" /> '''Complex of the enzym...)
Current revision (07:31, 17 March 2021) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2h5a.gif|left|200px]]<br /><applet load="2h5a" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="2h5a, resolution 1.72&Aring;" />
 
-
'''Complex of the enzyme PMM/PGM with xylose 1-phosphate'''<br />
 
-
==Overview==
+
==Complex of the enzyme PMM/PGM with xylose 1-phosphate==
-
Two complexes of the enzyme phosphomannomutase/phosphoglucomutase, (PMM/PGM) from Pseudomonas aeruginosa with a slow substrate and with an, inhibitor have been characterized by X-ray crystallography. Both ligands, induce an interdomain rearrangement in the enzyme that creates a highly, buried active site. Comparisons with enzyme-substrate complexes show that, the inhibitor xylose 1-phosphate utilizes many of the previously observed, enzyme-ligand interactions. In contrast, analysis of the ribose, 1-phosphate complex reveals a combination of new and conserved, enzyme-ligand interactions for binding. The ability of PMM/PGM to, accommodate these two pentose phosphosugars in its active site may be, relevant for future efforts towards inhibitor design.
+
<StructureSection load='2h5a' size='340' side='right'caption='[[2h5a]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2h5a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H5A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H5A FirstGlance]. <br>
 +
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=X1P:1-O-PHOSPHONO-ALPHA-D-XYLOPYRANOSE'>X1P</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 +
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</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;'>[[1k35|1k35]], [[1k2y|1k2y]], [[1p5d|1p5d]], [[1p5g|1p5g]], [[1pcj|1pcj]], [[1pcm|1pcm]], [[2h4l|2h4l]]</div></td></tr>
 +
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">algC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</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=2h5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h5a OCA], [https://pdbe.org/2h5a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h5a RCSB], [https://www.ebi.ac.uk/pdbsum/2h5a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h5a ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[[https://www.uniprot.org/uniprot/ALGC_PSEAE ALGC_PSEAE]] The phosphomannomutase activity produces a precursor for alginate polymerization. The alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core-LPS biosynthesis due to its phosphoglucomutase activity. Essential for rhamnolipid production, an exoproduct correlated with pathogenicity, and for biofilm production.<ref>PMID:7515870</ref> <ref>PMID:10481091</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/h5/2h5a_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=2h5a ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Two complexes of the enzyme phosphomannomutase/phosphoglucomutase (PMM/PGM) from Pseudomonas aeruginosa with a slow substrate and with an inhibitor have been characterized by X-ray crystallography. Both ligands induce an interdomain rearrangement in the enzyme that creates a highly buried active site. Comparisons with enzyme-substrate complexes show that the inhibitor xylose 1-phosphate utilizes many of the previously observed enzyme-ligand interactions. In contrast, analysis of the ribose 1-phosphate complex reveals a combination of new and conserved enzyme-ligand interactions for binding. The ability of PMM/PGM to accommodate these two pentose phosphosugars in its active site may be relevant for future efforts towards inhibitor design.
-
==About this Structure==
+
Complexes of the enzyme phosphomannomutase/phosphoglucomutase with a slow substrate and an inhibitor.,Regni C, Shackelford GS, Beamer LJ Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Aug 1;62(Pt, 8):722-6. Epub 2006 Jul 24. PMID:16880541<ref>PMID:16880541</ref>
-
2H5A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with ZN and X1P as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2H5A OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
Complexes of the enzyme phosphomannomutase/phosphoglucomutase with a slow substrate and an inhibitor., Regni C, Shackelford GS, Beamer LJ, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2006 Aug 1;62(Pt, 8):722-6. Epub 2006 Jul 24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16880541 16880541]
+
</div>
-
[[Category: Pseudomonas aeruginosa]]
+
<div class="pdbe-citations 2h5a" style="background-color:#fffaf0;"></div>
-
[[Category: Single protein]]
+
-
[[Category: Beamer, L.J.]]
+
-
[[Category: Regni, C.]]
+
-
[[Category: Shackelford, G.S.]]
+
-
[[Category: X1P]]
+
-
[[Category: ZN]]
+
-
[[Category: enzyme-ligand complex]]
+
-
[[Category: inhibitor]]
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:32:48 2007''
+
==See Also==
 +
*[[Phosphomannomutase|Phosphomannomutase]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
 +
[[Category: Beamer, L J]]
 +
[[Category: Regni, C]]
 +
[[Category: Shackelford, G S]]
 +
[[Category: Enzyme-ligand complex]]
 +
[[Category: Inhibitor]]
 +
[[Category: Isomerase]]

Current revision

Complex of the enzyme PMM/PGM with xylose 1-phosphate

PDB ID 2h5a

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2h5a"
Personal tools