View source for 4mks


==Crystal structure of enolase from Lactobacillus gasseri==
<StructureSection load='4mks' size='340' side='right'caption='[[4mks]], [[Resolution|resolution]] 2.08&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4mks]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactobacillus_gasseri_ATCC_33323_=_JCM_1131 Lactobacillus gasseri ATCC 33323 = JCM 1131]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MKS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MKS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.079&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=4mks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mks OCA], [https://pdbe.org/4mks PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mks RCSB], [https://www.ebi.ac.uk/pdbsum/4mks PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mks ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ENO2_LACGA ENO2_LACGA] Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Enolases are highly conserved metalloenzymes ubiquitous to cellular metabolism. While these enzymes share a large degree of sequence and structural similarity, they have been shown to possess a wide range of moonlighting functions. Recent studies showed that an enolase from Lactobacillus gasseri impedes the ability of Neisseria gonorrhoeae to adhere to epithelial cells. We present the crystal structure of this enolase, the first from Lactobacillus, with one of its Mg2+ cofactors. Determined using molecular replacement to 2.08A, the structure has a flexible and surface exposed catalytic loop containing lysines, and may play a role in the inhibitory function.

Crystal structure of an efficacious gonococcal adherence inhibitor: An enolase from Lactobacillus gasseri.,Raghunathan K, Harris PT, Spurbeck RR, Arvidson CG, Arvidson DN FEBS Lett. 2014 May 21. pii: S0014-5793(14)00392-5. doi:, 10.1016/j.febslet.2014.05.020. PMID:24859038<ref>PMID:24859038</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4mks" style="background-color:#fffaf0;"></div>

==See Also==
*[[Enolase 3D structures|Enolase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Lactobacillus gasseri ATCC 33323 = JCM 1131]]
[[Category: Large Structures]]
[[Category: Arvidson CG]]
[[Category: Arvidson DN]]
[[Category: Harris PT]]
[[Category: Raghunathan K]]
[[Category: Spurbeck RR]]