2azp: Difference between revisions

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<StructureSection load='2azp' size='340' side='right' caption='[[2azp]], [[Resolution|resolution]] 2.13&Aring;' scene=''>
<StructureSection load='2azp' size='340' side='right' caption='[[2azp]], [[Resolution|resolution]] 2.13&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2azp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AZP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AZP FirstGlance]. <br>
<table><tr><td colspan='2'>[[2azp]] is a 1 chain structure with sequence from [http://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=2AZP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AZP FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2azp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2azp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2azp RCSB], [http://www.ebi.ac.uk/pdbsum/2azp PDBsum], [http://www.topsan.org/Proteins/MCSG/2azp TOPSAN]</span></td></tr>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2azp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2azp OCA], [http://pdbe.org/2azp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2azp RCSB], [http://www.ebi.ac.uk/pdbsum/2azp PDBsum], [http://www.topsan.org/Proteins/MCSG/2azp TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/HYPRE_PSEAE HYPRE_PSEAE]] Allows intracellular utilization of 4-hydroxyproline, one of the major constituents of host collagen, by converting 4-hydroxy-L-proline to 4-hydroxy-D-proline, which can be further metabolized by intracellular 4-hydroxy-D-proline oxidases. Strong B-cell mitogen. Plays an important role in the regulation of intra- and extracellular amino acid pools, allowing the bacterium to profit from host precursors and enzymatic pathways.  
[[http://www.uniprot.org/uniprot/4HYPE_PSEAE 4HYPE_PSEAE]] Allows intracellular utilization of 4-hydroxyproline, one of the major constituents of host collagen, by converting trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp), which can be further metabolized by intracellular 4-hydroxy-D-proline oxidases. Strong B-cell mitogen. Plays an important role in the regulation of intra- and extracellular amino acid pools, allowing the bacterium to profit from host precursors and enzymatic pathways. Cannot use L-proline, trans-3-hydroxy-L-proline (t3LHyp) and pyrrolidone-5-carboxylate (P5C) as substrate.<ref>PMID:17849014</ref> <ref>PMID:20665524</ref> <ref>PMID:24980702</ref> 
== 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/chain_selection.php?pdb_ID=2ata 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/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Pseudomonas aeruginosa]]
[[Category: Edwards, A]]
[[Category: Edwards, A]]
[[Category: Gorodichtchenskaia, E]]
[[Category: Gorodichtchenskaia, E]]

Revision as of 19:11, 11 September 2015

Crystal Structure of PA1268 Solved by Sulfur SADCrystal Structure of PA1268 Solved by Sulfur SAD

Structural highlights

2azp is a 1 chain structure with sequence from "bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, TOPSAN

Function

[4HYPE_PSEAE] Allows intracellular utilization of 4-hydroxyproline, one of the major constituents of host collagen, by converting trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp), which can be further metabolized by intracellular 4-hydroxy-D-proline oxidases. Strong B-cell mitogen. Plays an important role in the regulation of intra- and extracellular amino acid pools, allowing the bacterium to profit from host precursors and enzymatic pathways. Cannot use L-proline, trans-3-hydroxy-L-proline (t3LHyp) and pyrrolidone-5-carboxylate (P5C) as substrate.[1] [2] [3]

Evolutionary Conservation

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

References

  1. ↑ Goytia M, Chamond N, Cosson A, Coatnoan N, Hermant D, Berneman A, Minoprio P. Molecular and structural discrimination of proline racemase and hydroxyproline-2-epimerase from nosocomial and bacterial pathogens. PLoS One. 2007 Sep 12;2(9):e885. PMID:17849014 doi:http://dx.doi.org/10.1371/journal.pone.0000885
  2. ↑ Gavina JM, White CE, Finan TM, Britz-McKibbin P. Determination of 4-hydroxyproline-2-epimerase activity by capillary electrophoresis: A stereoselective platform for inhibitor screening of amino acid isomerases. Electrophoresis. 2010 Aug;31(16):2831-7. doi: 10.1002/elps.201000187. PMID:20665524 doi:http://dx.doi.org/10.1002/elps.201000187
  3. ↑ Zhao S, Sakai A, Zhang X, Vetting MW, Kumar R, Hillerich B, San Francisco B, Solbiati J, Steves A, Brown S, Akiva E, Barber A, Seidel RD, Babbitt PC, Almo SC, Gerlt JA, Jacobson MP. Prediction and characterization of enzymatic activities guided by sequence similarity and genome neighborhood networks. Elife. 2014 Jun 30;3. doi: 10.7554/eLife.03275. PMID:24980702 doi:http://dx.doi.org/10.7554/eLife.03275

2azp, resolution 2.13Å

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