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.


1p31

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (05:52, 17 April 2024) (edit) (undo)
 
(12 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1p31.jpg|left|200px]]<br /><applet load="1p31" size="350" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1p31, resolution 1.85&Aring;" />
 
-
'''Crystal Structure of UDP-N-acetylmuramic acid:L-alanine Ligase (MurC) from Haemophilus influenzae'''<br />
 
-
==Overview==
+
==Crystal Structure of UDP-N-acetylmuramic acid:L-alanine Ligase (MurC) from Haemophilus influenzae==
-
UDP-N-acetylmuramic acid:L-alanine ligase (MurC) catalyzes the addition of the first amino acid to the cytoplasmic precursor of the bacterial cell wall peptidoglycan. The crystal structures of Haemophilus influenzae MurC in complex with its substrate UDP-N-acetylmuramic acid (UNAM) and Mg(2+) and of a fully assembled MurC complex with its product UDP-N-acetylmuramoyl-L-alanine (UMA), the nonhydrolyzable ATP analogue AMPPNP, and Mn(2+) have been determined to 1.85- and 1.7-A resolution, respectively. These structures reveal a conserved, three-domain architecture with the binding sites for UNAM and ATP formed at the domain interfaces: the N-terminal domain binds the UDP portion of UNAM, and the central and C-terminal domains form the ATP-binding site, while the C-terminal domain also positions the alanine. An active enzyme structure is thus assembled at the common domain interfaces when all three substrates are bound. The MurC active site clearly shows that the gamma-phosphate of AMPPNP is positioned between two bound metal ions, one of which also binds the reactive UNAM carboxylate, and that the alanine is oriented by interactions with the positively charged side chains of two MurC arginine residues and the negatively charged alanine carboxyl group. These results indicate that significant diversity exists in binding of the UDP moiety of the substrate by MurC and the subsequent ligases in the bacterial cell wall biosynthesis pathway and that alterations in the domain packing and tertiary structure allow the Mur ligases to bind sequentially larger UNAM peptide substrates.
+
<StructureSection load='1p31' size='340' side='right'caption='[[1p31]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
-
 
+
== Structural highlights ==
-
==About this Structure==
+
<table><tr><td colspan='2'>[[1p31]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P31 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P31 FirstGlance]. <br>
-
1P31 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=EPU:'>EPU</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/UDP-N-acetylmuramate--L-alanine_ligase UDP-N-acetylmuramate--L-alanine ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.8 6.3.2.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P31 OCA].
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
-
 
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPU:URIDINE-DIPHOSPHATE-2(N-ACETYLGLUCOSAMINYL)+BUTYRIC+ACID'>EPU</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-
==Reference==
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1p31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p31 OCA], [https://pdbe.org/1p31 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p31 RCSB], [https://www.ebi.ac.uk/pdbsum/1p31 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p31 ProSAT]</span></td></tr>
-
Crystal structures of active fully assembled substrate- and product-bound complexes of UDP-N-acetylmuramic acid:L-alanine ligase (MurC) from Haemophilus influenzae., Mol CD, Brooun A, Dougan DR, Hilgers MT, Tari LW, Wijnands RA, Knuth MW, McRee DE, Swanson RV, J Bacteriol. 2003 Jul;185(14):4152-62. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12837790 12837790]
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/MURC_HAEIN MURC_HAEIN] Cell wall formation.
 +
== 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/p3/1p31_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=1p31 ConSurf].
 +
<div style="clear:both"></div>
 +
__TOC__
 +
</StructureSection>
[[Category: Haemophilus influenzae]]
[[Category: Haemophilus influenzae]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: UDP-N-acetylmuramate--L-alanine ligase]]
+
[[Category: Brooun A]]
-
[[Category: Brooun, A.]]
+
[[Category: Dougan DR]]
-
[[Category: Dougan, D R.]]
+
[[Category: Hilgers MT]]
-
[[Category: Hilgers, M T.]]
+
[[Category: Knuth MW]]
-
[[Category: Knuth, M W.]]
+
[[Category: McRee DE]]
-
[[Category: McRee, D E.]]
+
[[Category: Mol CD]]
-
[[Category: Mol, C D.]]
+
[[Category: Swanson RV]]
-
[[Category: Swanson, R V.]]
+
[[Category: Tari LW]]
-
[[Category: Tari, L W.]]
+
[[Category: Wijnands RA]]
-
[[Category: Wijnands, R A.]]
+
-
[[Category: EPU]]
+
-
[[Category: MG]]
+
-
[[Category: alpha/beta protein]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:24:34 2008''
+

Current revision

Crystal Structure of UDP-N-acetylmuramic acid:L-alanine Ligase (MurC) from Haemophilus influenzae

PDB ID 1p31

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/1p31"
Personal tools